NOVEL COMPOUNDS AND THERAPEUTIC USES THEREOF

20230322815 · 2023-10-12

    Inventors

    Cpc classification

    International classification

    Abstract

    The present invention relates to compounds of Formula I:

    ##STR00001##

    wherein R.sup.1, L.sup.1, A, X.sup.a, L.sup.2, B and X.sup.b are each as defined herein. The present invention also relates to compounds of Formula II and III defined herein, formed by self-assembly of the compounds of Formula I with a metal M and an anion Q. Compounds of Formula II and III are useful in the treatment of proliferative disorders, such as cancer. The present invention also relates to pharmaceutical compositions comprising compounds of Formula I, II or III, and to the use of these compounds and compositions in the treatment of proliferative disorders, such as cancer.

    Claims

    1. A compound having a structure according to Formula I shown below, or a pharmaceutically acceptable salt, hydrate or solvate thereof, for use as a medicament: ##STR00089## wherein R.sup.1 is selected from the group consisting of N, CR.sup.2, aryl, heteroaryl, carbocyclyl and heterocyclyl, where any aryl, heteroaryl, carbocyclyl or heterocyclyl in R.sup.1 is optionally substituted with one or more R.sup.3; each R.sup.3 is independently selected from the group consisting of hydroxy, cyano, halogen, (1-4C)alkyl, (1-4C)haloalkyl, (2-4C)alkenyl, (2-4C)alkynyl, aryl, aryl(1-3C)alkyl, heteroaryl, heteroaryl(1-3C)alkyl, carbocyclyl, carbocyclyl(1-3C)alkyl, heterocyclyl, heterocyclyl(1-3C)alkyl, —OR.sup.3a, —NR.sup.3aR.sup.3b, —C(O)—R.sup.3a, —C(O)—OR.sup.3a, —O—C(O)—R.sup.3a, —C(O)—NR.sup.3aR.sup.3b, —N(R.sup.3a)C(O)—R.sup.3b and —S(O).sub.0-2R.sup.3a, where any (1-4C)alkyl, (1-4C)haloalkyl, (2-4C)alkenyl, (2-4C)alkynyl, aryl, aryl(1-3C)alkyl, heteroaryl, heteroaryl(1-3C)alkyl, carbocyclyl, carbocyclyl(1-3C)alkyl, heterocyclyl or heterocyclyl(1-3C)alkyl in R.sup.3 is optionally substituted with one or more R.sup.3c; R.sup.3a and R.sup.3b are each independently selected from the group consisting of hydrogen, (1-3C)alkyl and (1-3C)haloalkyl; each R.sup.3c is independently selected from the group consisting of hydroxy, halogen, cyano, amino, (1-3C)alkyl, (1-3C)alkoxy and (1-3C)haloalkyl; R.sup.2 is selected from the group consisting of hydrogen, hydroxy, cyano, halogen, (1-4C)alkyl, (1-4C)haloalkyl, (2-4C)alkenyl, (2-4C)alkynyl, aryl, aryl(1-3C)alkyl, heteroaryl, heteroaryl(1-3C)alkyl, carbocyclyl, carbocyclyl(1-3C)alkyl, heterocyclyl, heterocyclyl(1-3C)alkyl, —OR.sup.2a, —NR.sup.2aR.sup.2b, —C(O)—R.sup.2a, —C(O)—OR.sup.2a, —O—C(O)—R.sup.2a, —C(O)—NR.sup.2aR.sup.2b, —N(R.sup.2a)C(O)—R.sup.2b and —S(O).sub.0-2R.sup.9a, where any (1-4C)alkyl, (1-4C)haloalkyl, (2-4C)alkenyl, (2-4C)alkynyl, aryl, aryl(1-3C)alkyl, heteroaryl, heteroaryl(1-3C)alkyl, carbocyclyl, carbocyclyl(1-3C)alkyl, heterocyclyl or heterocyclyl(1-3C)alkyl in R.sup.2 is optionally substituted with one or more R.sup.2c; R.sup.2a and R.sup.2b are each independently selected from the group consisting of hydrogen, (1-3C)alkyl and (1-3C)haloalkyl; each R.sup.2c is independently selected from the group consisting of hydroxy, halogen, cyano, amino, (1-3C)alkyl, (1-3C)alkoxy and (1-3C)haloalkyl; each L.sup.1 is a group:
    —(W).sub.n—(X).sub.m—(Y).sub.o—(Z).sub.p— in which n and o are each independently 0, 1 or 2, and m and p are each independently 0 or 1, with the provisos that when m and p are both 1, o is not 0; each W is selected from the group consisting of (1-3C)alkylene, (2-3C)alkenylene, (2-3C)alkynylene, arylene, heteroarylene, carbocyclylene and heterocyclylene, where any (1-3C)alkylene, (2-3C)alkenylene, (2-3C)alkynylene, arylene, heteroarylene, carbocyclylene or heterocyclylene in W is optionally substituted with one or more W.sup.a, where each W.sup.a is independently selected from the group consisting of hydroxy, cyano, halogen, amino, (1-2)alkoxy and (1-2C)haloalkyl; X is selected from the group consisting of —O—, —C(O)—, —C(O)—O—, —O—C(O)—, —S(O).sub.0-2—, —C(O)—N(R.sup.x)—, —N(R.sup.x)—C(O)—, —NR.sup.x—, —N(R.sup.x)—C(O)—NR.sup.x—, —SO.sub.2N(R.sup.x)—, and —N(R.sup.x)SO.sub.2, where each R.sup.x is independently selected from the group consisting of hydrogen, hydroxy, cyano, (1-4C)alkyl, (2-4C)alkenyl and (2-4C)alkynyl; each Y is selected from the group consisting of (1-3C)alkylene, (2-3C)alkenylene, (2-3C)alkynylene, arylene, heteroarylene, carbocyclylene and heterocyclylene, where any (1-3C)alkylene, (2-3C)alkenylene, (2-3C)alkynylene, arylene, heteroarylene, carbocyclylene or heterocyclylene in Y is optionally substituted with one or more Y.sup.a, where each Y.sup.a is independently selected from the group consisting of hydroxy, cyano, halogen, amino, (1-2)alkoxy and (1-2C)haloalkyl; Z is selected from the group consisting of —O—, —C(O)—, —C(O)—O—, —O—C(O)—, —S(O).sub.0-2—, —C(O)—N(R.sup.z)—, —N(R.sup.z)—C(O)—, —NR.sup.z—, —N(R.sup.z)—C(O)—NR.sup.z—, —SO.sub.2N(R.sup.z)—, and —N(R.sup.z)SO.sub.2, where each R.sup.z is independently selected from the group consisting of hydrogen, hydroxy, cyano, (1-4C)alkyl, (2-4C)alkenyl and (2-4C)alkynyl; X.sup.a is a ring heteroatom located within ring A and is selected from N and O; each ring A is a monocyclic heteroaryl, bicyclic heteroaryl, monocyclic heterocycle or bicyclic heterocycle, any one of which is optionally substituted with one or more R.sup.4, where each R.sup.4 is independently selected from the group consisting of hydroxy, cyano, halogen, (1-6C)alkyl, (1-6C)haloalkyl, (2-6C)alkenyl, (2-6C)alkynyl, aryl, aryl(1-3C)alkyl, heteroaryl, heteroaryl(1-3C)alkyl, carbocyclyl, carbocyclyl(1-3C)alkyl, heterocyclyl, heterocyclyl(1-3C)alkyl, —R.sup.4a—OR.sup.4b, —R.sup.4a—NR.sup.4bR.sup.4c, —R.sup.4a—C(O)—R.sup.4b, —R.sup.4a—C(O)—OR.sup.4b, —R.sup.4a—O—C(O)—R.sup.4b, —R.sup.4a—C(O)—NR.sup.4bR.sup.4c, —R.sup.4a—N(R.sup.4b)C(O)—R.sup.4c and —R.sup.4a—S(O).sub.0-2R.sup.4b, where any (1-6C)alkyl, (1-6C)haloalkyl, (2-6C)alkenyl, (2-6C)alkynyl, aryl, aryl(1-3C)alkyl, heteroaryl, heteroaryl(1-3C)alkyl, carbocyclyl, carbocyclyl(1-3C)alkyl, heterocyclyl or heterocyclyl(1-3C)alkyl in R.sup.4 is optionally substituted with one or more R.sup.4d; R.sup.4a is absent or is (1-3C)alkylene that is optionally substituted with one or substituents selected from group consisting of hydroxy, halo and amino; R.sup.4b and R.sup.4c are each independently selected from the group consisting of hydrogen, (1-3C)alkyl and (1-3C)haloalkyl; each R.sup.4d is independently selected from the group consisting of hydroxy, halogen, cyano, amino, (1-3C)alkyl, (1-3C)alkoxy and (1-3C)haloalkyl; X.sup.b is a ring heteroatom located within ring B and is selected from N and O each ring B is a monocyclic heteroaryl, bicyclic heteroaryl, monocyclic heterocycle or bicyclic heterocycle, any one of which is optionally substituted with one or more R.sup.5, where each R.sup.5 is independently selected from the group consisting of hydroxy, cyano, halogen, (1-6C)alkyl, (1-6C)haloalkyl, (2-6C)alkenyl, (2-6C)alkynyl, aryl, aryl(1-3C)alkyl, heteroaryl, heteroaryl(1-3C)alkyl, carbocyclyl, carbocyclyl(1-3C)alkyl, heterocyclyl, heterocyclyl(1-3C)alkyl, —R.sup.5a—OR.sup.5b, —R.sup.5a—NR.sup.5bR.sup.5c, —R.sup.5a—C(O)—R.sup.5b, —R.sup.5a—C(O)—OR.sup.5b, —R.sup.5a—O—C(O)—R.sup.5b, —R.sup.5a—C(O)—NR.sup.5bR.sup.5c, —R.sup.5a—N(R.sup.5b)C(O)—R.sup.5c and —R.sup.5a—S(O).sub.0-2R.sup.5b, where any (1-6C)alkyl, (1-6C)haloalkyl, (2-6C)alkenyl, (2-6C)alkynyl, aryl, aryl(1-3C)alkyl, heteroaryl, heteroaryl(1-3C)alkyl, carbocyclyl, carbocyclyl(1-3C)alkyl, heterocyclyl or heterocyclyl(1-3C)alkyl in R.sup.5 is optionally substituted with one or more R.sup.5d; R.sup.5a is absent or is (1-3C)alkylene that is optionally substituted with one or substituents selected from group consisting of hydroxy, halo and amino; R.sup.5b and R.sup.5c are each independently selected from the group consisting of hydrogen, (1-5C)alkyl (e.g. (1-3C)alkyl) and (1-3C)haloalkyl; each R.sup.5d is independently selected from the group consisting of hydroxy, halogen, cyano, amino, (1-3C)alkyl, (1-3C)alkoxy and (1-3C)haloalkyl; and each L.sup.2 is selected from the group consisting of absent (in which case ring A is bonded directly to ring B), (1-2C)alkylene, ethenylene and ethynylene, where any (1-2C)alkylene, ethenylene and ethynylene in L.sup.2 is optionally substituted with one or more substituents selected form the group consisting of hydroxy, halogen, cyano, amino, (1-3C)alkyl, (1-3C)alkoxy and (1-3C)haloalkyl; and wherein the compound of Formula I, or the pharmaceutically acceptable salt, hydrate or solvate thereof, is for use in combination with a source of M, wherein M is selected from the group consisting of Zn.sup.2+, Mn.sup.2+, Cu.sup.2+, Fe.sup.2+, CO.sup.2+ and Ni.sup.2+.

    2. The compound, pharmaceutically acceptable salt, hydrate or solvate for use according to claim 1, wherein each ring A is a 5-6 membered monocyclic heteroaryl containing 1, 2 or 3 ring heteroatoms in total independently selected from N, O and S, or a 5-6 membered monocyclic heterocycle containing 1, 2 or 3 ring heteroatoms in total independently selected from N, O and S, wherein each ring A is optionally substituted with one or more R.sup.4, and X.sup.a is located immediately adjacent the carbon atom bonded to L.sup.1;

    3. The compound, pharmaceutically acceptable salt, hydrate or solvate for use according to claim 1 or 2, wherein each ring B is: i) a 5-6 membered monocyclic heterocycle containing 1, 2 or 3 ring heteroatoms in total that are independently selected from N, O and S; ii) a 5-6 membered monocyclic heteroaryl containing 1, 2 or 3 ring heteroatoms in total that are independently selected from N, O and S; iii) a 9-10 membered bicyclic heterocycle containing 1, 2 or 3 ring heteroatoms in total that are independently selected from N, O and S; or iv) a 9-10 membered bicyclic heteroaryl containing 1, 2 or 3 ring heteroatoms in total that are independently selected from N, O and S, wherein any ring in B is optionally substituted with one or more R.sup.5, and X.sup.b is located immediately adjacent the carbon atom bonded to L.sup.2.

    4. The compound, pharmaceutically acceptable salt, hydrate or solvate for use according to claim 1, 2 or 3, wherein each ring A is group: ##STR00090## wherein a is 0 or 1.

    5. The compound, pharmaceutically acceptable salt, hydrate or solvate for use according to any preceding claim, wherein each ring B is any of the following: ##STR00091## wherein: b.sup.1 is 0, 1 or 2, and b.sup.2 is 0, 1, 2 or 3.

    6. The compound, pharmaceutically acceptable salt, hydrate or solvate for use according to any preceding claim, wherein each W is selected from the group consisting of (1-3C)alkylene or phenylene, where any (1-3C)alkylene or phenylene in W is optionally substituted with one or more W.sup.a; X is selected from the group consisting of —C(O)—N(R.sup.x)—, —N(R.sup.x)—C(O)— and —NR.sup.x—; each Y is selected from the group consisting of (1-3C)alkylene or phenylene, where any (1-3C)alkylene or phenylene in Y is optionally substituted with one or more Y.sup.a; and Z is selected from the group consisting of —C(O)—N(R.sup.z)—, —N(R.sup.z)—C(O)— and —NR.sup.z—.

    7. The compound, pharmaceutically acceptable salt, hydrate or solvate for use according to any preceding claim, wherein: n is 0 or 1 and W is selected from the group consisting of (1-3C)alkylene or phenylene, where any (1-3C)alkylene or phenylene in W is optionally substituted with one or more W.sup.a, where each W.sup.a is independently selected from the group consisting of hydroxy, halogen, (1-2)alkoxy and (1-2C)haloalkyl; m is 0; o is 0 or 1 and Y is selected from the group consisting of (1-3C)alkylene or phenylene, where any (1-3C)alkylene or phenylene in Y is optionally substituted with one or more Y.sup.a, where each Y.sup.a is independently selected from the group consisting of hydroxy, halogen, (1-2)alkoxy and (1-2C)haloalkyl; and p is 1 and Z is —NR.sup.z—, where R.sup.z is hydrogen.

    8. The compound, pharmaceutically acceptable salt, hydrate or solvate for use according to any preceding claim, wherein: n is 0 or 1 and W is selected from the group consisting of (1-3C)alkylene or phenylene, where any (1-3C)alkylene or phenylene in W is optionally substituted with one or more W.sup.a, where each W.sup.a is independently selected from the group consisting of hydroxy, halogen, (1-2)alkoxy and (1-2C)haloalkyl; m is 0; o is 0 or 1 and Y is selected from the group consisting of (1-3C)alkylene or phenylene, where any (1-3C)alkylene or phenylene in Y is optionally substituted with one or more Y.sup.a, where each Y.sup.a is independently selected from the group consisting of hydroxy, halogen, (1-2)alkoxy and (1-2C)haloalkyl; and p is 1 and Z is —NR.sup.z—, where R.sup.z is hydrogen.

    9. The compound, pharmaceutically acceptable salt, hydrate or solvate for use according to any preceding claim, wherein L.sup.1 has a structure according to any one of the following: ##STR00092##

    10. The compound, pharmaceutically acceptable salt, hydrate or solvate for use according to any preceding claim, wherein L.sup.2 is selected from the group consisting of absent and (1-2C)alkylene, where any (1-2C)alkylene in L.sup.2 is optionally substituted with one or more substituents selected form the group consisting of hydroxy, halogen and (1-2C)haloalkyl.

    11. The compound, pharmaceutically acceptable salt, hydrate or solvate for use according to any preceding claim, wherein R.sup.1 is selected from the group consisting of N, CR.sup.2, phenyl and cyclohexyl, where any phenyl or cyclohexyl in R.sup.1 is optionally substituted with one or more R.sup.3; each R.sup.3 is independently selected from the group consisting of hydroxy, halogen, (1-4C)alkyl, (1-4C)haloalkyl and —OR.sup.3a, where any (1-4C)alkyl or (1-4C)haloalkyl in R.sup.3 is optionally substituted with one or more R.sup.3c; R.sup.2 is selected from the group consisting of hydrogen, and (1-3C)alkyl, where any (1-4C)alkyl in R.sup.2 is optionally substituted with one or more R.sup.2c.

    12. The compound, pharmaceutically acceptable salt, hydrate or solvate for use according to any preceding claim, wherein R.sup.1 has a structure according to any one of the following: ##STR00093##

    13. The compound, pharmaceutically acceptable salt, hydrate or solvate for use according to any preceding claim, wherein R.sup.5b and R.sup.5c are each independently selected from the group consisting of hydrogen, (1-3C)alkyl and (1-3C)haloalkyl.

    14. The compound, pharmaceutically acceptable salt, hydrate or solvate for use according to any preceding claim, wherein M is selected from the group consisting of Zn.sup.2+, Cu.sup.2+, Mn.sup.2+ and Fe.sup.2+.

    15. The compound, pharmaceutically acceptable salt, hydrate or solvate for use according to any preceding claim, wherein the compound of Formula I, or a pharmaceutically acceptable salt, hydrate or solvate thereof, is in further combination with a source of Q, wherein Q is an anion selected from the group consisting of spherical monoanionic anions, trigonal planar anions, dianionic tetrahedral anions, trianionic tetrahedral anions, dianionic octahedral anions and trianionic octahedral anions.

    16. The compound, pharmaceutically acceptable salt, hydrate or solvate for use according to claim 15, wherein Q is an anion selected from the group consisting of dianionic tetrahedral oxoanions and trianionic tetrahedral oxoanions.

    17. The compound, pharmaceutically acceptable salt, hydrate or solvate for use according to claim 15 or 16, wherein Q is sulfate (SO.sub.4.sup.2−), phosphate (PO.sub.4.sup.3−) or organophosphate (such as monophenylphosphate).

    18. The compound, pharmaceutically acceptable salt, hydrate or solvate for use according to any preceding claim, wherein the compound of Formula I has a structure according to any one of the following: ##STR00094## ##STR00095## ##STR00096## ##STR00097## or a pharmaceutically-acceptable salt, hydrate and/or solvate thereof.

    19. The compound, pharmaceutically acceptable salt, hydrate or solvate for use according to any preceding claim, wherein the compound of Formula I has the structure: ##STR00098## or a pharmaceutically-acceptable salt, hydrate and/or solvate thereof.

    20. A compound having a structure according to Formula II shown below, or a pharmaceutically acceptable salt, hydrate or solvate thereof, for use as a medicament: ##STR00099## wherein M, R.sup.1, L.sup.1, A, X.sup.a, L.sup.2, B, X.sup.b and any associated subgroups are as defined in any preceding claim.

    21. The compound, pharmaceutically acceptable salt, hydrate or solvate for use according to claim 20, wherein the compound of Formula II, or a pharmaceutically acceptable salt, hydrate or solvate thereof, is in further combination with a source of Q as defined in any one of claims 15, 16 and 17.

    22. The compound, pharmaceutically acceptable salt, hydrate or solvate for use according to claim 20 or 21, wherein the compound of Formula II has a structure according to any one of the following: ##STR00100## or a pharmaceutically-acceptable salt, hydrate and/or solvate thereof.

    23. A compound having a structure according to Formula III shown below, or a pharmaceutically acceptable salt, hydrate or solvate thereof, for use as a medicament: ##STR00101## wherein M, Q, R.sup.1, L.sup.1, A, X.sup.a, L.sup.2, B, X.sup.b and any associated subgroups are as defined in any one of claims 1-19.

    24. The compound, pharmaceutically acceptable salt, hydrate or solvate for use according to claim 23, wherein the compound of Formula III has a structure according to any one of the following: ##STR00102## or a pharmaceutically-acceptable salt, hydrate and/or solvate thereof.

    25. The compound, pharmaceutically acceptable salt, hydrate or solvate for use according to any preceding claim, wherein the medicament is for the treatment of a proliferative disorder (e.g. cancer).

    Description

    EXAMPLES

    [0599] One or more examples of the invention will now be described, for the purpose of illustration only, with reference to the accompanying figures:

    [0600] FIG. 1. Mononuclear complexes of L. a, structure of [LZn].sup.2+. b, [LMn(H.sub.2O).sub.2].sup.2+.

    [0601] FIG. 2. Self-assembled metal-containing complexes of L incorporating SO.sub.4.sup.2−. a, X-ray structure of [L.sub.2Zn.sub.3(SO.sub.4)].sup.4+. b, [L.sub.2Zn.sub.3(SO.sub.4)].sup.4+ with ligands coloured for clarity. c, X-ray structure of [L.sub.2Mn.sub.3(H.sub.2O).sub.2(SO.sub.4)].sup.4+. d, [L.sub.2Mn.sub.3(H.sub.2O).sub.2(SO.sub.4)].sup.4+ with ligands coloured for clarity.

    [0602] FIG. 3. Self-assembled Cu.sup.2+ complexes of L incorporating PhOPO.sub.3.sup.2−. a, X-ray structure of [L.sub.2Cu.sub.3(PhOPO.sub.3)].sup.4+. b, [L.sub.2Cu.sub.3(PhOPO.sub.3)].sup.4+ with ligands coloured for clarity.

    [0603] FIG. 4. Reaction of [L.sub.2Zn.sub.3].sup.6+ and [L.sub.2Mn.sub.3].sup.6+ with PhOPO.sub.3.sup.2−. a, X-ray structure of [L.sub.2Zn.sub.3 (PO.sub.4)].sup.3+. b, [L.sub.2Zn.sub.3(PO.sub.4)].sup.3+ with ligands coloured for clarity. c, X-ray structure of [L.sub.2Mn.sub.3 (H.sub.2O).sub.2(PO.sub.4)].sup.3+. d, [L.sub.2Mn.sub.3(H.sub.2O).sub.2(PO.sub.4)].sup.3+ with ligands coloured for clarity.

    [0604] FIG. 5. a, ESI-MS of [L.sub.2Cu.sub.3(PhOPO.sub.3)](ClO.sub.4).sub.4. b, ESI-MS of [L.sub.2Cu.sub.3(PhOPO.sub.3)](ClO.sub.4).sub.4 after being heated at 80° C. for 1 hour. c, ESI-MS of [L.sub.2Zn.sub.3(PhOPO.sub.3)](ClO.sub.4).sub.4. d, ESI-MS of [L.sub.2Zn.sub.3(PhOPO.sub.3)](ClO.sub.4).sub.4 after being heated at 80° C. for 1 hour.

    [0605] FIG. 6. Phosphatase activity of [L.sub.2Zn.sub.3].sup.6+. .sup.31P NMR spectra using different substrates including PhOPO.sub.3 (spectra A to D), serine phosphate (spectra E to H), threonine phosphate (spectra I to L) and tyrosine phosphate (spectra M to P). Specific details for each .sup.31P NMR spectra are as follows: Spectra A, E, I and M represent substrate alone (44 hrs incubated @ 37° C.); Spectra B, F, J and N represents [L.sub.2Zn.sub.3].sup.6+ plus substrate (t=0 min); Spectra C, G, K and O represents [L.sub.2Zn.sub.3].sup.6+ plus substrate incubated @ 37° C. for 19 hours; Spectra D, H, L and M represents [L.sub.2Zn.sub.3].sup.6+ plus substrate incubated @ 37° C. for 44 hours. The .sup.31P NMR of [L.sub.2Zn.sub.3(PO.sub.4)].sup.3+ gives a signal at 8.6 ppm. The doubling up of some of the .sup.31P signals in [L.sub.2Zn.sub.3(PO.sub.4)].sup.3+ (H, P and L) is attributed to formation of a mixture of diastereoisomers between the racemic cryptand and the resolved chiral amino acids which will form an ion-pair ([L.sub.2Zn.sub.3(PO.sub.4)](RCH(NH.sub.2)CO.sub.2).sup.2+) and does not occur with the achiral phenyl phosphate.

    [0606] FIG. 7. Chemosensitivity response of a panel of human cancer and non-cancer cell lines to 96 h continuous exposure to self-assembling test compounds. a, The potency of compounds tested against cancer (HT-29, DLD-1, HCT116 p53.sup.+/+ and p53+, PSN1, MiaPaCa2, BxPC3, A549, H460 and GBM1) and non-cancer cells (ARPE-19, MCF10A and NP1). Each value represents the mean IC.sub.50±standard deviation from a minimum of three independent experiments. b,c, The selectivity index (SI) for [L.sub.2Cu.sub.3].sup.6+ (b) and [L.sub.2Zn.sub.3].sup.6+ (c) for the indicated cancer cell lines; SI is defined as the mean IC.sub.50 against the particular non-cancer cell line model divided by the mean IC.sub.50 against the particular cancer cell line. SI values >1 indicate that the test compound is more active against the particular cancer cell line than the corresponding non-cancer cells. As the SI value is calculated using the mean IC.sub.50 values, experimental error is not included in these figures. d,e, IC.sub.50 values for the clinically approved platinates (cisplatin, oxaliplatin and carboplatin) and [L.sub.2Mn.sub.3].sup.6+ and the corresponding SI results.

    [0607] FIG. 8. Effect of the complex anion on potency and selectivity. a, The effect of various anions on the potency of the Zn.sup.2+ complex; this is expressed as relative potency which is defined as the IC.sub.50 of [L.sub.2Zn.sub.3(PO.sub.4)].sup.3+, [L.sub.2Zn.sub.3 (SO.sub.4)].sup.4+ or [L.sub.2Zn.sub.3 (O.sub.3POPh)].sup.4+ divided by the IC.sub.50 of [L.sub.2Zn.sub.3].sup.6+ (values <1 and >1 indicate increased and decreased potency respectively). b, Effects of the anion on selectivity; these results are expressed as relative SI defined as the SI of [L.sub.2Zn.sub.3(PO.sub.4)].sup.3+, [L.sub.2Zn.sub.3(SO.sub.4)].sup.4+ or [L.sub.2Zn.sub.3(O.sub.3POPh)].sup.4+ divided by the SI of [L.sub.2Zn.sub.3].sup.6+ (values >1 and <1 indicate increased and decreased selectivity respectively).

    [0608] FIG. 9. Effects of [L.sub.2Zn.sub.3].sup.6+ and [L.sub.2Cu.sub.3].sup.6+ on the activity of purified human kinases. a,b, Percentage inhibition of the indicated kinases by [L.sub.2Zn.sub.3].sup.6+ (a) and [L.sub.2Cu.sub.3].sup.6+ (b) respectively at a concentration of 10 μM; full results are presented in the ESI. c,d, Kinases whose activity is stimulated by [L.sub.2Zn.sub.3].sup.6+ (c) or [L.sub.2Cu.sub.3].sup.6+ (d) complexes. e,f, Kinome map showing kinases inhibited (red) or stimulated (green) by [L.sub.2Zn.sub.3].sup.6+ (e) or [L.sub.2Cu.sub.3].sup.6+ (f). III ustration reproduced courtesy of Cell Signalling Technology Inc (www.cellsignal.com)

    [0609] FIG. 10. Western blot analysis of purified recombinant Src and AMPK following exposure to [L.sub.2Zn.sub.3].sup.6+ and [L.sub.2Cu.sub.3].sup.6+. Purified enzymes were incubated with complexes (50 μM) for 4 hours in the presence of ATP prior to analysis.

    [0610] FIG. 11. Effects of [L.sub.2Zn.sub.3].sup.6+, [L.sub.2Cu.sub.3].sup.6+ and [L.sub.2Mn.sub.3].sup.6+ complexes on autophagy and cellular ATP levels. a, Representative fluorescent images showing CYTO-ID autophagic staining (green) and Hoechst (blue) with bright field overlay of HCT116 p53.sup.−/− cells treated with 3.125 μM [L.sub.2Zn.sub.3].sup.6+, [L.sub.2Cu.sub.3].sup.6+ or [L.sub.2Mn.sub.3].sup.6+ for 40 h. White arrows indicate intracellular vacuoles. b, Cellular ATP levels in ARPE19 non-cancer cells and HCT116 p53.sup.+/+ cancer cells with 20 h exposure to [L.sub.2Zn.sub.3].sup.6+ at the indicated concentrations.

    [0611] FIG. 12. Immunoblots showing the differential effects of [L.sub.2Cu.sub.3].sup.6+ and [L.sub.2Zn.sub.3].sup.6+ treatment of HCT116 cancer cells and ARPE19 non-cancer cells on key cellular proteins associated with cellular and metabolic stress. Representative immunoblot images of the indicated proteins following cell exposure to 5 μM [L.sub.2Cu.sub.3].sup.6+ or [L.sub.2Zn.sub.3].sup.6+ for 40 h. Tyrosine phosphorylated proteins are indicated using a pan-phospho-Tyr antibody; β-actin as a loading control.

    [0612] FIG. 13. The effect of anions of the potency of [L.sub.2Cu.sub.3].sup.6+ and [L.sub.2Zn.sub.3].sup.6+. The results represent the mean IC.sub.50 values ±standard deviation for at least three independent experiments.

    [0613] FIG. 14. The effect of anions on the selectivity of [L.sub.2Cu.sub.3].sup.6+ and [L.sub.2Zn.sub.3].sup.6+. All values presented here were determined from the mean IC.sub.50 values in FIG. 13 for each of the non-cancer cell lines used in this study. As a result, no error bars are presented here as the experimental error is accounted for in FIG. 13.

    [0614] FIG. 15. The effect of anions on the potency and selectivity relative to [L.sub.2Cu.sub.3].sup.6+ and [L.sub.2Zn.sub.3].sup.6+. Relative potency was determined by dividing the IC.sub.50 of test compounds plus respective anions divided by IC.sub.50 values for [L.sub.2Cu.sub.3].sup.6+ and [L.sub.2Zn.sub.3].sup.6+. Values >1 represent an increase in potency and conversely, values <1 represent a reduction in potency. Relative selectivity index (SI) values were determined by dividing the SI value for test compounds plus respective anions divided by SI values for [L.sub.2Cu.sub.3].sup.6+ and [L.sub.2Zn.sub.3].sup.6+. Values >1 represent an increase in selectivity and conversely, values <1 represent a reduction in selectivity.

    [0615] FIG. 16. The effect of [L.sub.2Zn.sub.3].sup.6+ and [L.sub.2Cu.sub.3].sup.6+ on the activity of recombinant human kinases. The compounds were submitted to the MRC Protein Phosphorylation and Ubiquitination Unit International Centre for Kinase Profiling (University of Dundee) and tested at a concentration of 10 μM against 140 human kinases (Premier Screen).

    [0616] FIG. 17. The effects of [L.sub.2Cu.sub.3].sup.6+, [L.sub.2Zn.sub.3].sup.6+ and [L.sub.2Mn.sub.3].sup.6+ on cellular vacuole formation and autophagy in the HCT116 p53.sup.−/− cancer cells. Representative confocal images are shown of HCT116 p53.sup.−/− cancer cells following 40 h treatment with vehicle control or 3.125 μM [L.sub.2Cu.sub.3].sup.6+, [L.sub.2Zn.sub.3].sup.6+, or [L.sub.2Mn.sub.3].sup.6+. Upper panel shows phase contrast cell images with white arrows indicating intracellular vacuoles. Middle panel shows cells staining positive for autophagy (CYTO-ID autophagic dye, green). Lower panel shows overlay of phase contrast cell images with CYTO-ID autophagic staining (green, punctate, cytoplasmic) and counterstaining of nuclei (Hoechst).

    [0617] FIG. 18. The effects of [L.sub.2Cu.sub.3].sup.6+, [L.sub.2Zn.sub.3].sup.6+ and [L.sub.2Mn.sub.3].sup.6+ on cellular vacuole formation and autophagy in the HCT116 p53.sup.+/+ cancer cells. Representative confocal images are shown of HCT116 p53.sup.+/+ cancer cells following 40 h treatment with vehicle control or 3.125 μM [L.sub.2Cu.sub.3].sup.6+, [L.sub.2Zn.sub.3].sup.6+, or [L.sub.2Mn.sub.3].sup.6+. Upper panel shows phase contrast cell images with white arrows indicating intracellular vacuoles. Middle panel shows cells staining positive for autophagy (CYTO-ID autophagic dye, green). Lower panel shows overlay of phase contrast cell images with CYTO-ID autophagic staining (green, punctate, cytoplasmic) and counterstaining of nuclei (Hoechst).

    [0618] FIG. 19. The effects of [L.sub.2Cu.sub.3].sup.6+, [L.sub.2Zn.sub.3].sup.6+ and [L.sub.2Mn.sub.3].sup.6+ on cellular vacuole formation and autophagy in the ARPE19 non-cancer cells. Representative confocal images are shown of ARPE19 non-cancer cells following 40 h treatment with vehicle control or 3.125 μM [L.sub.2Cu.sub.3].sup.6+, [L.sub.2Zn.sub.3].sup.6+, or [L.sub.2Mn.sub.3].sup.6+. Upper panel shows cells staining positive for autophagy (CYTO-ID autophagic dye, green). Lower panel shows overlay of phase contrast cell images with CYTO-ID autophagic staining (green, punctate, cytoplasmic) and counterstaining of nuclei (Hoechst).

    [0619] FIG. 20. The effects of [L.sub.2Cu.sub.3].sup.6+, [L.sub.2Zn.sub.3].sup.6+ and [L.sub.2Mn.sub.3].sup.6+ on cellular ATP levels in the ARPE19 non-cancer and HCT116 p53.sup.+/+ cancer cells. The effects of 20 h treatment with the indicated concentrations of [L.sub.2Cu.sub.3].sup.6+, [L.sub.2Zn.sub.3].sup.6+, or [L.sub.2Mn.sub.3].sup.6+ on total cellular levels of ATP compared to levels in vehicle control-treated ARPE19 or HCT116.sup.+/+ cells. n=3 biological repeats, students t-test (p values).

    [0620] FIG. 21. Activity of [L.sub.2Cu.sub.3].sup.6+ and [L.sub.2Zn.sub.3].sup.6+ against primary H460 tumors. The results presented represent the mean tumour weight±SEM following treatment at 3 different doses of [L.sub.2Cu.sub.3].sup.6+ and [L.sub.2Zn.sub.3].sup.6+: L2Zn3 [1]=54 μM, L2Zn3 [2]=108 μM, L2Zn3 [3]=216 μM; L2Cu3 [1]=42 μM, L2Cu3[2]=84 μM, L2Cu3[3]=168 μM. SoC paclitaxel. Statistical analysis by one way ANOVA (*): 0.05≥p value >0.01; (**): 0.01≥p value >0.001; (***): 0.001≥p value; (****): 0.0001≥p value. Number per experimental group n=10-13.

    [0621] FIG. 22. Evaluation of the effects of [L.sub.2Cu.sub.3].sup.6+ and [L.sub.2Zn.sub.3].sup.6+ on primary H460 metastasis to the lower CAM. Relative ALU expression (relative to chicken GAPDH) as a quantitive marker of metastasis of human cells to the lower CAM. L2Zn3 [1]=54 μM, L2Zn3 [2]=108 μM, L2Zn3 [3]=216 μM; L2Cu3 [1]=42 μM, L2Cu3[2]=84 μM, L2Cu3[3]=168 μM. SoC paclitaxel. Relative expression ±SEM. Statistical analysis by one way ANOVA (*): 0.05≥p value >0.01; (**): 0.01≥p value >0.001; (***): 0.001≥p value; (****): 0.0001≥p value. Number per experimental group n=7-8.

    [0622] FIG. 23. Activity of [L.sub.2Cu.sub.3].sup.6+ and [L.sub.2Zn.sub.3].sup.6+ against primary HT29 tumors. The results presented represent the mean tumour weight ±SEM following treatment at 3 different doses of [L.sub.2Cu.sub.3].sup.6+ and [L.sub.2Zn.sub.3].sup.6+: L2Zn3 [1]=26.6 μM, L2Zn3 [2]=53.2 μM, L2Zn3 [3]=106.4 μM; L2Cu3 [1]=23.8 μM, L2Cu3[2]=65.7 μM, L2Cu3[3]=131.46 μM. SoC doxorubicin. Statistical analysis by one way ANOVA (*): 0.05≥p value >0.01; (**): 0.01≥p value >0.001; (***): 0.001≥p value; (****): 0.0001≥p value. Number per experimental group n=10-14.

    [0623] FIG. 24. Activity of [L.sub.2Cu.sub.3].sup.6+ and [L.sub.2Zn.sub.3].sup.6+ against primary HCT116 tumors. The results presented represent the mean tumour weight ±SEM following treatment at 3 different doses of [L.sub.2Cu.sub.3].sup.6+ and [L.sub.2Zn.sub.3].sup.6+: L2Zn3 [1]=70.5 μM, L2Zn3 [2]=141 μM, L2Zn3 [3]=282 μM; L2Cu3 [1]=75 μM, L2Cu3[2]=150 μM, L2Cu3[3]=300 μM. SoC doxorubicin. Statistical analysis by one way ANOVA (*): 0.05≥p value >0.01; (**): 0.01≥p value >0.001; (***): 0.001≥p value; (****): 0.0001≥p value. Number per experimental group n=12-15.

    [0624] FIG. 25. Evaluation of the effects of [L.sub.2Cu.sub.3].sup.6+ and [L.sub.2Zn.sub.3].sup.6+ on primary HCT116 metastasis to the lower CAM. Relative ALU expression (relative to chicken GAPDH) as a quantitive marker of metastasis of human cells to the lower CAM. Relative expression ±SEM. L2Zn3 [1]=70.5 μM, L2Zn3 [2]=141 μM, L2Zn3 [3]=282 μM; L2Cu3 [1]=75 μM, L2Cu3[2]=150 μM, L2Cu3[3]=300 μM. SoC doxorubicin. Number per experimental group n=7-8.

    PART A

    Synthesis and Characterisation

    [0625] Unless otherwise stated, all solvents and materials were purchased from either Sigma Aldrich, Fisher Scientific or Fluorochem and were used without further purification. .sup.1H, .sup.13C, DEPT-135 and DEPT-90 NMR data was recorded on either a Bruker Fourier 300 MHz or Bruker Avance III (AVIII) 400 MHz spectrometer or a Bruker Avance Neo 600 MHz NMR spectrometer. Mass spectra were obtained on an Agilent 6210 TOF MS with electrospray ionisation operating in positive ion mode and mass spectra of metal complexes were obtained on a Bruker Micro TOF-q LC mass spectrometer with electrospray ionisation operating in positive ion mode. Phosphorylated ‘SAMS’ peptide HMRSAMS*GLHLVKRR (phosphorylated on the serine residue) was obtained from PeptideSynthetics, Peptide Protein Research Ltd (>95% purity).

    [0626] Single crystal X-ray diffraction data was collected at 150(2) K on a Bruker D8 Venture diffractometer equipped with a graphite monochromated Mo(Kα) radiation source and a cold stream of N2 gas. Solutions were generated by conventional heavy atom Patterson or direct methods and refined by full-matrix least squares on all F.sup.2 data, using SHELXS-97 and SHELXL software respectively..sup.26 Absorption corrections were applied based on multiple and symmetry-equivalent measurements using SADABS..sup.27 Almost all the structures contained some form of disordered ether with solvent molecules and/or counter anions (generally substitutional or rotation disorder). In these cases, the atoms were modelled using the PART instruction in the least squares refinement and refined over two positions. The anisotropic displacement parameters were treated with S/MU, DELU and in some cases ISOR where needed. Due to the diffuse nature of the electron density map the hydrogen atoms were not added to disordered solvent molecules. The structure [L.sub.2Zn.sub.3SO.sub.4](BF.sub.4).sub.3.5 contained extensively disordered tetrafluoroborate counter anions, one of which refined poorly and was modelled with 50% occupancy.

    Ligand Synthesis

    Synthesis of L

    [0627] The ligand L was prepared as described previously..sup.28 However, procedures for the synthesis of the benzoylated thioamide (1) and the thioamide (2) were slightly modified.

    ##STR00087##

    [0628] Synthesis of (1): To a solution of tris(2-aminoethyl)amine (1.0 g, 6.84 mmol) in acetone (50 mL) under an atmosphere of dinitrogen was added benzoyl isothiocyanate (3.7 g, 22.6 mmol) at such a rate to cause the reaction to gently reflux. After addition the reaction was stirred overnight during which time a colourless precipitate formed. The precipitate was isolated by filtration and washed with acetone (3×5 mL) giving (1) as a white solid. Yield=2.05 g (47%). .sup.1H NMR (400 MHz, DMSO-d.sup.6) δ (ppm) 11.20 (s, 3H, —NH), 11.0 (t, 3H, J=4.8, —CH.sub.2Nh), 7.81 (d, 6H, J=7.2, Ph), 7.56 (t, 3H, J=7.4, Ph), 7.38 (t, 6H, J=7.6, Ph), 3.75 (q, 6H, J=5.7, —CH.sub.2CH.sub.2NH), 2.89 (t, 6H, J=6.0 Hz, —CH.sub.2CH.sub.2NH). .sup.13C NMR [100 MHz, DMSO-d.sup.6]: δ.sub.C=180.5 (C═S), 168.2 (C═O), 133.1 (CH), 132.7 (Q), 128.9 (CH), 128.6 (CH), 51.9 (CH.sub.2), 42.6 (CH.sub.2). ESI-MS m/z 636 (M+H.sup.+), HR ESI-MS found 636.1882 C.sub.30H.sub.33N.sub.7S.sub.3O.sub.3 requires 636.1880 (error 0.46 ppm).

    [0629] Synthesis of (2): The benzoylated urea derivative (1) (1.3 g, 2.05 mmol) was suspended in water (20 mL) and NaOH (820 mg, 20.5 mmol) added. The reaction was then heated to 60° C. and after 48 hrs the temperature was incrementally decreased allowing the solution to slowly cool to room temperature, avoiding formation on an oil and resulting in the formation of a colourless precipitate. Isolation by filtration and washing with ice cold water (2×1 mL) gave the tri-thiourea (2) as a colourless solid. Yield=503 mg (76%). .sup.1H NMR (400 MHz, DMSO-d.sup.6) δ (ppm) 7.55 (brs, 3H, —NH), 7.08 (brs, 6H, —NH.sub.2), 3.44 (brs, 6H, —CH.sub.2CH.sub.2NH), 2.58 (brs, 6H, —CH.sub.2CH.sub.2NH). .sup.13C NMR [100 MHz, DMSO-d.sup.6]: δ.sub.C=183.5 (C═S), 52.9 (CH.sub.2), 42.3 (CH.sub.2). ESI-MS m/z 324 (M+H.sup.+), HR ESI-MS found 324.1089 C.sub.9H.sub.21N.sub.7S.sub.3 requires 324.1093 (error 1.03 ppm).

    Synthesis of L.SUP.1

    [0630] Ligand L.sup.1 (an analogue of ligand L) shown below was prepared according to the following protocol.

    [0631] Synthesis of α-bromo-2-acetylisoquinoline: To a solution of 2-acetylisoquinoline (1.0 g, 6.28 mmol) in carbon tetrachloride (20 mL) at 80° C. was added liquid bromine (0.39 mL, 7.55 mmol) in carbon tetrachloride (0.6 mL) slowly and dropwise until TLC (SiO.sub.2, 1% MeOH in DCM) showed the absence of the starting material. The reaction was cooled, diluted in dichloromethane (100 mL) and washed strenuously with saturated sodium carbonate solution (2×50 mL). The organic layer was removed, dried over anhydrous magnesium sulfate and solvents removed by reduced pressure to leave the crude product as a yellow oil. This was purified by column chromatography (1% MeOH in DCM, SiO.sub.2) and solvents removed to leave the pure product as a slightly yellow oil (1.08 g, 72%). .sup.1H NMR (400 MHz, CDCl.sub.3) δ (ppm) 9.06-9.00 (m, 1H), 8.62 (d, J=5.5 Hz, 1H), 7.90-7.95 (m, 2H), 7.81-7.73 (m, 2H), 5.04 (s, 2H). .sup.13C NMR [100 MHz, CDCl.sub.3]: δ.sub.C=194.1 (Q), 150.1 (Q), 141.1 (CH), 137.1 (Q), 130.7 (CH), 129.7 (CH), 127.1 (CH), 126.53 (Q), 126.49 (CH), 125.6 (CH), 34.7 (CH.sub.2). ESI-MS m/z 249.9864 (M+H.sup.+), observed neutral mass 248.9788, C.sub.11H.sub.8NOBr requires 248.9789 (error 0.37 ppm).

    [0632] Synthesis of L.sup.1: To a solution of α-bromo-2-acetylisoquinoline (500 mg, 2.10 mmol) in ethanol (20 mL), 1,1′, 1″-(nitrilotris(ethane-2,1-diyl))tris(thiourea) (226 mg, 0.70 mmol) was added. The reaction was then heated to 80° C. for 12 h, during which time all the solid dissolved and the solution turned yellow. The solution was then allowed to cool and the solvent removed under reduced pressure. The resultant oil was diluted in dichloromethane (50 mL) and washed with saturated aqueous sodium bicarbonate solution (2×25 mL). The combined organic layers were dried over anhydrous magnesium sulfate and solvent removed under reduced pressure to give the crude product as a brown/yellow oil. This was purified by column chromatography (SiO.sub.2, 10% methanol in dichloromethane) to afford L.sup.1 as an orange solid (277 mg, 51%). .sup.1H NMR (400 MHz, CDCl.sub.3) δ (ppm) 8.88 (d, J=8.5, 3H), 8.56 (d, J=5.6, 3H), 7.81 (d, J=8.2, 3H), 7.64-7.57 (m, 6H), 7.48 (ddd, J=8.3, 7.1, 1.0, 3H), 7.09 (s, 3H), 6.39 (br s, 3H), 3.50 (q, J=5.3, 6H), 2.90 (t, J=5.56 Hz, 6H). .sup.13C NMR [100 MHz, CDCl.sub.3]: δ.sub.C=169.2 (Q), 153.7 (Q), 150.9 (Q), 142.0 (CH), 137.1 (Q), 129.9 (CH), 127.9 (CH), 127.1 (CH), 126.72 (Q), 126.70 (CH), 120.5 (CH), 108.8 (CH), 53.3 (CH.sub.2), 43.4 (CH.sub.2). ESI-MS m/z 777.2363 (M+H.sup.+), observed neutral mass 776.2291, C.sub.42H.sub.36N.sub.10S.sub.3 requires 776.2287 (error 0.63 ppm).

    ##STR00088##

    Synthesis of Complexes

    Mononuclear Complexes

    [0633] Synthesis of [LZn](ClO.sub.4).sub.2. To a solution of Zn(ClO.sub.4).sub.2.Math.6H.sub.2O (10 mg. 0.027 mmol) in MeCN (1 ml) was added a suspension of ligand L (12 mg, 0.019 mmol) in MeCN and the reaction sonicated until a clear solution had formed. To this was added water (˜1 ml) and the solution slowly allowed to evaporate, during which time pale yellow crystals were formed which were isolated by filtration and dried (yield=9 mg. 53%*). The [LMn](ClO.sub.4).sub.2 complex was prepared in an analogous fashion using Mn(ClO.sub.4).sub.2.Math.6H.sub.2O giving yellow crystals (yield=10 mg, 60%*). *percentage yield based on the moles of ligand used.

    Trinuclear Complexes

    [0634] Synthesis of [L.sub.2Zn.sub.3(SO.sub.4)](ClO.sub.4).sub.4. To a solution of Zn(ClO.sub.4).sub.2.Math.6H.sub.2O (10 mg. 0.027 mmol) in MeCN (1 ml) was added a suspension of ligand L (12 mg, 0.019 mmol) in MeCN and the reaction sonicated until a clear solution had formed. To this was added water (˜1 ml) containing Bu.sub.4NHSO.sub.4 (3.1 mg, 0.009 mmol) and the solution slowly allowed to evaporate during which time colourless crystals were formed which were isolated by filtration and dried (yield=11 mg, 60%). The [L.sub.2Mn.sub.3(SO.sub.4)](ClO.sub.4).sub.4 complex was prepared in an analogous fashion using Mn(ClO.sub.4).sub.2.Math.6H.sub.2O giving yellow crystals (yield=9 mg, 50%).

    [0635] Synthesis of [L.sub.2Cu.sub.3(O.sub.3POPh)](ClO.sub.4).sub.4. To a solution of Cu(ClO.sub.4).sub.2.Math.6H.sub.2O (10 mg. 0.027 mmol) in MeCN (1 ml) was added a suspension of ligand L (12 mg, 0.019 mmol) in MeCN and the reaction sonicated until a clear solution had formed. To this was added water (˜1 ml) containing Na.sub.2O.sub.3POPh (2.3 mg, 0.009 mmol) and the solution slowly allowed to evaporate giving green crystals which were isolated by filtration and dried (yield=9 mg, 47%).

    [0636] Synthesis of [L.sub.2Zn.sub.3(PO.sub.4)](ClO.sub.4).sub.3. To a solution of Zn(ClO.sub.4).sub.2.Math.6H.sub.2O (10 mg. 0.027 mmol) in MeCN (1 ml) was added a suspension of ligand L (12 mg, 0.019 mmol) in MeCN and the reaction sonicated until a clear solution had formed. To this was added water (˜1 ml) containing Na.sub.2O.sub.3POPh (2.3 mg, 0.009 mmol) and the solution slowly allowed to evaporate giving yellow crystals which were isolated by filtration and dried (yield=10 mg, 54%). The [L.sub.2Mn.sub.3(PO.sub.4)](ClO.sub.4).sub.3 complex was prepared in an analogous fashion using Mn(ClO.sub.4).sub.2.Math.6H.sub.2O giving yellow crystals (yield=9 mg, 50%).

    DISCUSSION

    [0637] Reaction of 1.5 equivalents of L with either Zn(ClO.sub.4).sub.2 or Mn(ClO.sub.4).sub.2 results in a mononuclear complex (e.g. [LM].sup.2+) as demonstrated by X-ray crystallography and ESI-MS. In the solid-state the zinc complex contains a 6-coordinate Zn.sup.2+ cation coordinated by six nitrogen atoms from three pyridyl-thiazole bidentate units from the same ligand. In the Mn.sup.2+ analogue the metal ion is again 6-coordinate, but this arises from coordination by four N-donor atoms from two bidentate pyridyl-thiazole units and two water O-donor atoms (FIG. 1). Both complexes differ from the Cu.sup.2+ derivative which can form the trimetallic capsule (e.g. [L.sub.2Cu.sub.3].sup.6+) even in the presence of weakly interacting anions. The difference is attributed to the ability of Cu.sup.2+ to form 4-coordinate complexes (at least with pyridyl-thiazole donors) whereas both Zn.sup.2+ and Mn.sup.2+ prefer higher-coordinate geometry and without a strongly coordinating anion present a simple mononuclear species is formed. The coordination of water in the Mn.sup.2+ complex (e.g. [LMn(H.sub.2O).sub.2].sup.2+) is a consequence of the oxophillic nature of this hard cation and this behaviour is mirrored in all the structures with this metal. The formation of these species is also observed in the gas phase with ESI-MS studies showing that only ions corresponding to the mononuclear species are present.

    [0638] Reaction of L with either Mn.sup.2+ or Zn.sup.2+ with (Bu.sub.4N)HSO.sub.4 (in the correct stoichiometric proportions) results in the formation of the capsule in which sulfate anions are encapsulated (e.g. [L.sub.2M.sub.3(SO.sub.4)].sup.4+) (FIG. 2). In the solid state the Zn.sup.2+ is isostructural to the Cu.sup.2+ derivative with a trinuclear [L.sub.2Zn.sub.3].sup.6+ assembly and within it is an encapsulated sulfate anion (e.g. [L.sub.3Zn(SO.sub.4)].sup.4+). Each of the three Zn.sup.2+ atoms are 5-coordinate arising from four N-donor atoms from two bidentate pyridyl-thiazole units and one oxygen donor from the sulfate anion. The sulfate is held within the capsule by three coordination bonds to Zn.sup.2+ supplemented by three —NH—O hydrogen bonding interactions. The remaining uncoordinated oxygen atom forms hydrogen bonds to three —NH donor units within the “upper rim” of the cavity. The Mn.sup.2+ forms a very similar type of assembly but each of the Mn.sup.2+ metal ions are 6-coordinate, which for one of the metal ions arises from four N-donor atoms from two bidentate pyridyl-thiazole units and two oxygen donors from the sulfate anion. The remaining two ions are also 6-coordinate and are coordinated by two bidentate N-donor ligands but are coordinated by one oxygen atom from the sulfate anion and one water molecule (e.g. [L.sub.2Mn.sub.3(H.sub.2O).sub.2(SO.sub.4)].sup.4+). This demonstrates that whilst with weakly interacting anions (e.g. halides, ClO.sub.4.sup.−, and BF.sub.4.sup.−) both Zn.sup.2+ and Mn.sup.2+ form mononuclear complexes, with tetrahedral oxoanions these template the formation of the trimetallic capsule.

    [0639] Ions in the ESI-MS at m/z 1844 and 1812 corresponding to {[L.sub.2Zn.sub.3(SO.sub.4)(ClO.sub.4).sub.3}.sup.+ and {[L.sub.2Mn.sub.3(SO.sub.4)(ClO.sub.4).sub.3}.sup.+ coupled with doubly charged ions indicate that these species are also observed in the gas phase.

    [0640] Addition of disodium phenylphosphate to a solution of [L.sub.2Cu.sub.3].sup.6+ in MeCN/H.sub.2O results in a colour change from light blue to green. Crystals were then deposited after several days and analysis by X-ray crystallography shows that the trimetallic capsule is still formed but held inside the host is a PhOPO.sub.3.sup.2− anion. In a very similar fashion to the other oxoanions, PhOPO.sub.3.sup.2− is coordinated to the three Cu.sup.2+ metal ions supplemented by a series of —NH— anion interactions. However, due to the phenyl substituent the ligands adopt a slightly different conformation allowing the phenyl unit to occupy a cleft formed by two pyridyl-thiazole units (FIG. 3).

    [0641] Reaction of two equivalents of L, three equivalents of either M(ClO.sub.4).sub.2(where M=Zn.sup.2+ or Mn.sup.2+) and PhOPO.sub.3Na.sub.2 results in a very different species. In the solid-state both structures contain a central PO.sub.4.sup.3− anion held within the molecule by a series of interactions between the metal ions and amine hydrogen atoms (FIG. 4). The [L.sub.2Mn.sub.3(PO.sub.4)].sup.3+ complex is similar to the sulfate analogue and the three 6-coordinate Mn.sup.2+ metal ions are coordinated by two bidentate N-donor ligand domains but one metal ion is coordinated by two oxygen atoms from the anion and the remaining two metal ions are coordinated by one anion oxygen atom and a water molecule. The [L.sub.2Zn.sub.3(PO.sub.4)].sup.3+ is slightly different from the sulfate analogue and one metal ion is 6-coordinate arising from coordination of two bidentate N-donor ligand units and two oxygen atoms of the anion. The remaining two metal ions are only 5-coordinate as only one oxygen atom from the anion interacts with the metal.

    [0642] This metal-dependent reactivity is also observed in the ESI-MS. Reaction of [L.sub.2Cu.sub.3](ClO.sub.4).sub.6 with PhOPO.sub.3Na.sub.2 in water and MeCN gives ions at m/z 1914, 1024, 788 and 463 corresponding to {[L.sub.2Cu.sub.3(PhOPO.sub.3)](ClO.sub.4).sub.3}+, {[LCu.sub.2(PhOPO.sub.3)](ClO.sub.4)}+, {[LCu](ClO.sub.4)}+ and {[LCu.sub.2(PhOPO.sub.3)]}.sup.2+. Heating this sample at 80° C. shows no change in the ESI-MS spectrum indicating that the phenylphosphate dianion remains intact. A similar reaction of PhOPO.sub.3Na.sub.2 with Zn(ClO.sub.4).sub.2 and L gave an ESI-MS with ions at m/z 1920 and 910 corresponding to {[L.sub.2Zn.sub.3(PhOPO.sub.3)](ClO.sub.4).sub.3}.sup.+ and {[L.sub.2Zn.sub.3(PhOPO.sub.3)](ClO.sub.4).sub.2}.sup.2+ respectively. Lower molecular weight ions at m/z 1029, 791 and 464 corresponding to {[LZn.sub.2(PhOPO.sub.3)](ClO.sub.4)}.sup.+, {[LZn](ClO.sub.4)}.sup.+ and {[LZn.sub.2(PhOPO.sub.3)]}.sup.2+ were also observed. However, heating this sample at 80° C. results in a dramatic change in the ESI-MS with the spectrum now much simplified with ions at m/z 1743 and 822 corresponding to {[L.sub.2Zn.sub.3(PO.sub.4)](ClO.sub.4).sub.2}.sup.+ and {[L.sub.2Zn.sub.3(PO.sub.4)](ClO.sub.4)}.sup.2+. This demonstrates that initially the Zn.sup.2+ containing complex reacts with phenyl phosphate dianion and in a similar fashion to the Cu.sup.2+ analogue and forms the trinuclear complex incorporating this anion (e.g. [L.sub.2Zn.sub.3(PhOPO.sub.3)].sup.4+). However, after either a few days at room temperature or heating at 80° C. for 1 hr the anion is hydrolysed and phosphate is encapsulated within the cryptand (see FIGS. 5a-5d). This hydrolysis is also confirmed by .sup.1H NMR as reaction of two equivalents of L, three equivalents of Zn(ClO.sub.4).sub.2 and PhOPO.sub.3Na.sub.2 initially gives a broad complex spectrum but after 1 hr at 80° C. gave a spectrum that contains signals corresponding to [L.sub.2Zn.sub.3(PO.sub.4)].sup.3+ accompanied with signals corresponding to the phenol hydrolysis product. Reaction with Mn(ClO.sub.4).sub.2 is similar to the Zn.sup.2+ analogue with ions in the ESI-MS corresponding to binding of phenyl phosphate observed initially (e.g. {[LMn.sub.2(PhOPO.sub.3)](ClO.sub.4)}.sup.+) but ions corresponding to hydrolysis (e.g. {[L.sub.2Mn.sub.3(PO.sub.4)](ClO.sub.4).sub.2}.sup.+ and {[L.sub.2Mn.sub.3(PO.sub.4)](ClO.sub.4)}.sup.2+) are observed after heating for 1 hr..sup.29

    [0643] The Zn.sup.2+ complex shows substrate specific differences in the rates of hydrolysis and its phosphatase activity. Analysis of the hydrolysis of phenyl phosphate dianion by the Zn.sup.2+ complex (in a 25%:75% mixture of DMSO and buffered H.sub.2O solution (HEPES pH 7.5)) by .sup.31P NMR shows a signal at −1.5 ppm corresponding to unhydrolysed PhOPO.sub.3.sup.2− at t=0 (FIG. 6, spectra B). After 19 hrs at 37° C. the major signal present is now observed at 8.6 ppm which is at an identical chemical shift to [L.sub.2Zn.sub.3(PO.sub.4)].sup.3+ and after 44 hrs virtually no signal corresponding to PhOPO.sub.3.sup.2− is observed (FIG. 6, spectra C, D). In a similar experiment using 4-nitrophenyl phosphate no 31P signals could be detected that corresponded to the starting material following mixing with the Zn.sup.2+ complex indicating almost immediate hydrolysis. Only [L.sub.2Zn.sub.3(PO.sub.4)].sup.3+ was observed, coupled with a rapid yellowing of the solution due to the formation of 4-nitrophenolate.

    [0644] Given the importance of protein phosphorylation in inter- and intra-cellular signalling and to cell function, and its common dysregulation in cancers,.sup.30, 31 it was next analysed whether the Zn.sup.2+ complex could dephosphorylate the phosphorylated amino acids serine, threonine and tyrosine. Indeed, the Zn.sup.2+ complex resulted in dephosphorylation of serine-PO.sub.3.sup.2− and tyrosine-OPO.sub.3.sup.2− at similar hydrolysis rates to PhOPO.sub.3.sup.2− with substantial hydrolysis occurring over 24 hrs and completion after 48 hrs (FIG. 6, spectra E-H; M-P). Dephosphorylation of the amino acid threonine-OPO.sub.3.sup.2− by the Zn.sup.2+ complex was much slower however and after 48 hrs threonine-OPO.sub.3.sup.2− was still the major species (FIG. 6, spectra I-L). Differences in reactivity towards different substrates can be attributed to both steric and electronic effects. The difference in reactivity towards phenyl phosphate compared to the 4-nitro derivative is likely a consequence of the electron-withdrawing nitro group, which will enhance the hydrolysis. Serine-PO.sub.3.sup.2−, tyrosine-OPO.sub.3.sup.2− and threonine-OPO.sub.3.sup.2− all have similar electronic properties but threonine has a methyl substituent close to the phosphorylated residue and it would seem likely this would result in unfavourable steric interactions upon binding of [L.sub.2Zn.sub.3].sup.6+ as the —CHCH.sub.3 unit would be housed deep in the cleft of the self-assembled species (see FIG. 3). It seems probable that this interaction would reduce the ability of the cryptand to bind the anion and hence reduce the hydrolysis rate. Both serine and tyrosine are less sterically demanding (tyrosine-OPO.sub.3.sup.2− is very similar to PhOPO.sub.3.sup.2− and serine-PO.sub.3.sup.2− has a less sterically demanding —CH.sub.2— unit in this position) and consequently are hydrolysed more rapidly.

    [0645] The rate of substrate hydrolysis is also dependent upon the metal used in the self-assembly process. The solid-state and ESI-MS data suggest that [L.sub.2Cu.sub.3].sup.6+ does not hydrolyse phenyl phosphate but incorporates this anion within the assembly e.g. [L.sub.2Cu.sub.3(PhOPO.sub.3)].sup.4+. Comparison of the reactivity of the Zn.sup.2+ species verses the Mn.sup.2+ by monitoring the hydrolysis of 4-nitrophenyl phosphate by UV-Vis spectroscopy shows after 24 hrs the Mn.sup.2+ has hydrolysed with three times more phosphate, indicating that the Mn.sup.2+ is more active than the Zn.sup.2+ complex.

    Biological Studies

    Cell Lines and Culture

    [0646] All cell lines used were maintained at low passage in antibiotic-free media and were obtained from ATCC (LGC Standards, Middlesex, UK) unless otherwise stated (Methods). HT29, DLD-1, HCT116 p53.sup.+/+ and HCT116 p53.sup.−/− are all colorectal adenocarcinoma cell lines derived from different individuals and harbor different combinations of oncogenic lesions (except for the HCT116 isogenic cancer cell clones that are genetically identical except for p53 status). PSN-1, BxPC-3 and MiaPaCa2 are pancreatic carcinoma cell lines and A549 and H460 are lung carcinoma cell lines. HT29, DLD-1, PSN-1, BxPC-3, A549 and H460 cell lines were cultured in RPMI-1640 growth media (Sigma) containing 2 mM L-glutamine, 1 mM sodium pyruvate and 10% fetal bovine serum (FBS). HCT116 (p53.sup.+/+ and p53.sup.−/−) and MiaPaCa2 cell lines were cultured in Dulbecco's Modified Eagle's Medium (Sigma), 2 mM L-glutamine and 10% FBS. The ARPE-19 retinal epithelial non-cancer cell line (Dunn et al., 1996) was cultured in DMEM/F12 media (Gibco), 2 mM L-glutamine, 1 mM sodium pyruvate and 10% FBS. The MCF10A non-cancerous human breast epithelial cell line was cultured in Minimal Essential Media Eagle (Sigma), 2 mM L-glutamine, 1 mM sodium pyruvate, 10% FBS and 1×non-essential amino acids (NEAA). NP1 and GBM1 cells were cultured on plasticware coated with poly-L-ornithine (5 μg/ml) and laminin (2.4 μg/ml) (Polson et al., 2018; Da Silva et al., 2019). NP1 cells were grown in DMEM/F12 media (Gibco) supplemented with 5% FBS, 20 ng/ml hFGF, 20 ng/ml rhEGF, 0.5×B-27 supplement (Gibco), 0.5×N-2 supplement (Gibco) and 1×GLUTAMAX (Gibco). GBM1 cells were cultured in Neurobasal media (Gibco) supplemented with 40 ng/ml hFGF, 40 ng/ml rhEGF, 0.5×B-27 supplement (Gibco) and 0.5×N-2 supplement (Gibco).

    Chemosensitivity Studies

    [0647] [L.sub.2M.sub.3].sup.6+ and all the other self-assembling complexes were freshly formed by adding DMSO to individual components mixing together by pipetting. These were then further diluted in cell culture media such that the final DMSO concentration that cells were exposed to was 0.2% (vehicle control). Cisplatin, oxaliplatin and carboplatin were dissolved in phosphate buffered saline. Cell lines were seeded into 96 well plates at 2×10.sup.3 cells per well and incubated overnight at 37° C. GBM1 cancer stem-like cells were seeded at 3×10.sup.3 cells per well and NP1 neural progenitors were seeded at 1.5×10.sup.3 cells per well. The following day, media was removed and replaced with fresh media containing test compounds at a range of concentrations. Cells were incubated with test compounds for a further 96 hours after which the media was removed and replaced with fresh media (200 μl/well). MTT was added (20 μl at 5 mg/ml) and cells were incubated for a further 4 hours. Media and MTT were removed and formazan crystals were dissolved in 150 μl of DMSO and the absorbance of the resulting solution determined at 540 nm. Dose response curves were constructed, and the concentration required to reduce cell growth by 50% (IC.sub.50) determined. The selectivity index was defined as the IC.sub.50 for non-cancer cells divided by the IC.sub.50 for cancer cell lines with values >1 representing selectivity for cancer cells as opposed to non-cancer cells.

    Immunoblotting

    [0648] Protein lysates and recombinant proteins were resolved on 15% SDS polyacrylamide gels. Proteins were electroblotted onto nitrocellulose membrane by wet transfer in 1×Tris Glycine buffer (Biorad) at 35 mA overnight at room temperature (Allison et al., 2014). After blocking of membranes, these were incubated with primary antibody overnight at 4° C. before addition of rabbit or mouse secondary antibody (HRP-conjugated) for 1 h at room temperature and development of blots by enhanced chemiluminescence. Primary antibodies were: anti-Src (total) (Cell Signalling Technology #2123 1:1000), anti-phosphorylated Src (Y527) (Cell Signalling Technology #21055 1:1000), anti-phosphorylated Src (Y416) (Cell Signalling Technology #69435 1:1000), anti-AMPKα (total) (Cell Signalling Technology #2532 1:1000), anti-phosphorylated AMPKα (T172) (Cell Signalling Technology #2532 1:1000), anti-phospho-Tyr (pan) (Cell Signalling Technology #8954 1:2000), anti-p53 (Santa Cruz, DO-1 clone, 1:1000), anti-β-actin (Merck MAB1501, 1:40,000). Quantification of signals was performed by densitometry using Image J software.

    Results and Discussion

    [0649] [L.sub.2Cu.sub.3].sup.6+ and [L.sub.2Zn.sub.3].sup.6+ possess both potent and selective activity against most of the cancer cell lines tested compared to three non-cancer cell models utilised (FIG. 6, a-c). For [L.sub.2Zn.sub.3].sup.6+, IC.sub.50 values towards the cancer cell lines ranged from 70±13 nM against HCT116 p53.sup.−/− and up to 59.07±5.60 μM against MiaPaCa2. IC.sub.50 values for both complexes were mostly sub-μM towards cancer cells (HT-29, DLD-1, HCT116 (p53 wild type and null), BxPC3, A549 and H460 cell lines) with the exceptions being the pancreatic cancer cell line PSN1 and the GBM1 glioblastoma cancer stem cell model.sup.32,33 where IC.sub.50 values were >1 μM. Cancer stem cells are typically chemoresistant,.sup.34 however, importantly both complexes showed preferential activity towards the GBM1 cells compared to all three non-cancer cell models which included adult human brain progenitor cells (NP1)..sup.32,33 The MiaPaCa2 pancreatic cancer cell line was however inherently resistant to both complexes with IC.sub.50 values >10 μM (FIG. 7a).

    [0650] The magnitude of selectivity towards cancer cells was marked and for both [L.sub.2Cu.sub.3].sup.6+ and [L.sub.2Zn.sub.3].sup.6+ was over 10-fold for most of the cancer cell lines compared to all three non-cancer cell models (FIG. 7b,c). Remarkably, for [L.sub.2Zn.sub.3].sup.6+ selectivity indices of over 2000 were obtained in the case of HCT116 p53.sup.−/− cancer cells compared to ARPE-19 and MCF10A non-cancer cells (FIG. 7c). For the [L.sub.2Cu.sub.3].sup.6+ complex, selectivity indices for many of the cancer cell lines were >100 with the [L.sub.2Zn.sub.3].sup.6+ complex resulting in even higher SIs. Interestingly, however, whereas activity of the [L.sub.2Cu.sub.3].sup.6+ complex was very similar against the three non-cancer cell models, the NP1 brain progenitor cells.sup.32,33 showed increased sensitivity to the Zn.sup.2+ complex.

    [0651] Whilst the potency of both the Zn.sup.2+ and Cu.sup.2+ complexes (FIG. 7a) compares favourably with that of the clinically approved platinates (FIG. 7d), selectivity of the complexes is significantly superior under the same in vitro experimental conditions (FIG. 7b,c cf. 6e). In contrast, the Mn.sup.2+ complex, although a potent cytotoxin in vitro (FIG. 7d), it showed only modest preferential selectivity (˜2-fold) towards cancer cells which was comparable to that of the platinates (FIG. 7e).

    [0652] The encapsulation of different specific anions (e.g. PO.sub.4.sup.3−, SO.sub.4.sup.2− or PhOPO.sub.3.sup.2−) into the [L.sub.2Zn.sub.3].sup.6+ and [L.sub.2Cu.sub.3].sup.6+ complexes at the point of self-assembly prior to any cell exposure impacts on both activity and selectivity. The effect is both anion and cell line dependent (see FIG. 8 and Further results section) with the inclusion of different anions having either minimal effect or causing an increase or decrease in potency depending on the cell line. Against the PSN1 cell line for example, both [L.sub.2Zn.sub.3(SO.sub.4)].sup.4+ and [L.sub.2Zn.sub.3(O.sub.3POPh)].sup.4+ are significantly more active than [L.sub.2Zn.sub.3(PO.sub.4)].sup.3+ or [L.sub.2Zn.sub.3].sup.6+ and this translates into improved selectivity indices compared against the ARPE-19 cell line (FIG. 8). A similar but smaller increase in potency was also observed against HCT116 p53.sup.+/+ (but not the p53 null variant) and H460 cells treated with [L.sub.2Zn.sub.3(SO.sub.4)].sup.4+ and [L.sub.2Zn.sub.3(O.sub.3POPh)].sup.4+ leading to a corresponding increase in relative selectivity. In contrast, the inclusion of anions reduced the activity of [L.sub.2Zn.sub.3].sup.6+ against HT-29, DLD-1, BxPC3 and A549 cells resulting in a corresponding reduction in relative selectivity (FIG. 8). Similar results were obtained with [L.sub.2Cu.sub.3].sup.6+ complexes with PO.sub.4.sup.3−, SO.sub.4.sup.2− or PhOPO.sub.3.sup.2− anions (see Further results section). The mechanistic basis for these differential effects requires further investigation. However, these results demonstrate that the activity of these complexes can be readily modulated or potentially ‘tuned’ towards different cancer cells by altering the metal and/or the anion providing an inherently flexible platform for drug discovery.

    Mechanistic Studies

    [0653] Given the ability of the Zn.sup.2+ complex to dephosphorylate amino acids serine, tyrosine and threonine (FIG. 6) and the Cu.sup.2+ complex to bind phenyl phosphate (FIG. 3), it was examined whether the complexes affect the activity of kinases. This was assessed in a cell-free screen of 140 kinases using purified recombinant human kinases and substrate peptides incubated in the presence of .sup.33P ATP and 10 μM complex or solvent control. [L.sub.2Zn.sub.3].sup.6+ and [L.sub.2Cu.sub.3].sup.6+ inhibited the activity of multiple kinases to differing extents, with the most potently inhibited kinases being inhibited by near to 100% (FIG. 9a,b). [L.sub.2Cu.sub.3].sup.6+ has inhibitory activity against a larger number of kinases than [L.sub.2Zn.sub.3].sup.6+ which may reflect the fact that selectivity indices for [L.sub.2Cu.sub.3].sup.6+ are comparatively lower than those for [L.sub.2Zn.sub.3].sup.6+. In some cases, there is selective inhibition of specific kinases by either [L.sub.2Zn.sub.3].sup.6+ or [L.sub.2Cu.sub.3].sup.6+ (see Further results section). Across the kinome, the inhibition of kinases in the TK and CAMK family for [L.sub.2Zn.sub.3].sup.6+ and the CAMK and AGC family for [L.sub.2Cu.sub.3].sup.6+ were observed (FIG. 10e,f), however whether this reflects an overall preference of the compounds requires further investigation. For a few kinases, activity was increased by [L.sub.2Cu.sub.3].sup.6+ or [L.sub.2Zn.sub.3].sup.6+ (FIG. 9c,d), the most striking example being that of the proto-oncogene Src, a non-receptor tyrosine kinase..sup.35

    [0654] There are several potential mechanisms which could lead the observed kinase inhibition ‘readout’ of this screen including, i) direct ATP hydrolysis by the complex(es) and differing Km of the kinases for ATP, and, ii) dephosphorylation of the peptide substrate by the phosphatase activity of the Zn.sup.2+ complex resulting in cycles of peptide phosphorylation by active recombinant enzyme and dephosphorylation by the complex. However, mass spectroscopy showed little or no hydrolysis of ATP when incubated with Zn.sup.2+ or Cu.sup.2+ complex alone (see Further results section). Similarly, neither complex resulted in dephosphorylation of a purified phosphorylated AMPK peptide (see Further results section) although AMPK is one of the most potently inhibited kinases by both complexes (FIG. 9a,b).

    [0655] An alternative explanation of the observed effects which can be reconciled with both selective kinase inhibition and activation is that that the Zn.sup.2+ and Cu.sup.2+ complexes are modulating key regulatory phosphor-sites on the kinases themselves leading to enhanced or repressed kinase activity. In the case of the Zn.sup.2+ complex, dephosphorylation of specific phosphorylated regulatory amino acids through its phosphatase activity (FIG. 6) may lead to either kinase inhibition or activation. For the Cu.sup.2+ complex, it was hypothesised that it may bind to specific phosphorylated amino acids given its ability to bind but not hydrolyse phenyl phosphate (FIG. 3, see Further results section). This could affect kinase activity through influencing docking or binding of other proteins (eg. SH2-domain-containing activating or inhibitory proteins).sup.36 and through steric or structural effects.

    [0656] To investigate these hypotheses further, regulatory phospho-amino acids of two key kinases identified by the kinase screen, AMPK and Src, were analysed following incubation of the recombinant kinases with Zn.sup.2+ or Cu.sup.2+ complexes. Phosphorylation of AMPKα at threonine 172 (p-T172) stimulates AMPK activity.sup.37 and treatment of AMPK with either [L.sub.2Zn.sub.3].sup.6+ or [L.sub.2Cu.sub.3].sup.6+ significantly reduced p-T172 levels detectable by immunoblotting at a molecular weight of ˜63 kDa (FIG. 10).

    [0657] These results are consistent with the inhibition of AMPK by both [L.sub.2Zn.sub.3].sup.6+ and [L.sub.2Cu.sub.3].sup.6+ observed in the kinase screen (FIG. 9a,b) but subtle differences in mechanisms are revealed. In the case of [L.sub.2Cu.sub.3].sup.6+, high molecular weight bands of >250 kDa are detected with the p-T172 specific Src antibody suggesting that this compound is binding to the kinase, consistent with its ability to bind or encapsulate phosphoanionic molecules (eg. phenyl phosphate, FIG. 3). [L.sub.2Zn.sub.3].sup.6+ on the other hand causes a clear reduction in p-T172 and no high molecular weight bands consistent with phosphatase activity towards this phosphorylated amino acid of recombinant AMKPα (FIG. 6).

    [0658] For Src, effects of the complexes on two key regulatory phospho-amino acids were examined, Y527 and Y416 (FIG. 10). Phosphorylation at Y527 in the Src C-terminal domain is known to decrease Src activity whereas autophosphorylation at Y416 in the activation loop of the kinase domain increases Src activity..sup.36,38 Here, incubation of recombinant Src with [L.sub.2Zn.sub.3].sup.6+ resulted in a ˜30% decrease in p-Y527 relative to total Src levels and a ˜5-fold increase in p-Y416 levels (FIG. 10), both of which combined would be expected to result in enhanced Src kinase activity as was observed in the kinase screen (FIG. 9c,d). The decrease in p-Y527 is consistent with the selective phosphatase activity of [L.sub.2Zn.sub.3].sup.6+. Y527 dephosphorylation reduces allosteric inhibition of Src kinase activity by the C-terminal domain, enabling autophosphorylation of Src at Y416..sup.35 Similar to AMPK, incubation of [L.sub.2Cu.sub.3].sup.6+ with Src resulted in higher molecular weight bands detected with the total Src antibody which were not observed with control or [L.sub.2Zn.sub.3].sup.6+ treatments, suggesting binding of [L.sub.2Cu.sub.3].sup.6+ to Src. p-Y416 could not be detected raising the possibility that [L.sub.2Cu.sub.3].sup.6+ binding to Src masks detection of this epitope, however, further studies are required to unravel the detailed mechanism as to how [L.sub.2Cu.sub.3].sup.6+ binding to Src may increase its activity.

    Selective Induction of Autophagy and Cancer Cell ATP Depletion

    [0659] Given the kinase screen results indicating that the [L.sub.2Cu.sub.3].sup.6+ and [L.sub.2Zn.sub.3].sup.6+ complexes can inhibit multiple kinases as well as activating several others (FIG. 9 and see Further results section) and the dysregulation of phospho-signalling in cancers,.sup.31, 39 this provides a likely mechanism by which they exert their cancer selective activity. Phenotypically, [L.sub.2Zn.sub.3].sup.6+ induced the appearance of vacuoles in the HCT116 p53.sup.+/+ and p53.sup.−/− cancer cells which were shown to be autophagic using the established autophagic tracer dye CYTO-ID..sup.40 The Mn.sup.2+ complex also induced autophagy whereas [L.sub.2Cu.sub.3].sup.6+ did not (FIG. 11a, and see Further results section).

    [0660] Autophagy is a catabolic process that is induced in response to metabolic stresses including low ATP levels and starvation..sup.37 It was hypothesised that the induction of autophagy by Zn.sup.2+ and Mn.sup.2+ complexes could be due to cellular ATP depletion resulting from their protein phosphatase activity and repeated futile cycles between protein phosphorylation by constitutively active oncogenic kinases.sup.39 and dephosphorylation by the complexes. In support of this hypothesis, Zn.sup.2+ and Mn.sup.2+ complexes both caused a dose-dependent decrease in ATP levels (FIG. 11b and see ESI). This was much more pronounced in the HCT116 cancer cells than in ARPE19 non-cancerous cells with [L.sub.2Zn.sub.3].sup.6+, indicating cancer selective ATP depletion correlating with the excellent cancer cell selectivity indices of the Zn.sup.2+ complex (FIG. 7c). There was less difference in the magnitude of ATP depletion between the HCT116 cancer cells and the ARPE19 non-cancer cells with Mn.sup.2+ complex treatment (see Further results section), consistent with its more modest selectivity indices (FIG. 7d). This may relate to more promiscuous phosphatase activity of the Mn.sup.2+ complex or its higher rates of hydrolysis (see Further results section).

    [0661] Immunoblot analyses suggest that the autophagy is a compensatory catabolic response to sustain ATP levels and prevent bioenergetic failure and death with [L.sub.2Zn.sub.3].sup.6+ inducing activation of the ‘low ATP’ sensing kinase AMPK.sup.37 in HCT116 cancer cells but not in ARPE19 non-cancer cells (FIG. 12).

    [0662] Thus, cellular levels of p-T172 of AMPKα were increased relative to total AMPKα levels specifically in the HCT116 cancer cells by [L.sub.2Zn.sub.3].sup.6+ but not by [L.sub.2Cu.sub.3].sup.6+ (FIG. 12). T172 AMPKα phosphorylation is induced by low cellular ATP levels and increased AMP or ADP levels, enabling competitive binding of AMP/ADP to the y regulatory subunit of AMPK enabling AMPKα phosphorylation by one of the AMPK upstream kinases and blocking phosphatase access to p-T172..sup.37 Thus, paradoxically, [L.sub.2Zn.sub.3].sup.6+ causes dephosphorylation of T172 AMPKα and kinase inhibition in a cell-free system (ATP present) (FIG. 9a, 10) consistent with its phosphatase activity (FIG. 6) but results in increased cellular levels of p-T172 AMPK selectively in cancer cells (FIG. 12) which is attributed to selective ATP depletion (FIG. 11).

    [0663] Following [L.sub.2Zn.sub.3].sup.6+ treatment of HCT116 cancer cells, a small decrease (˜10%) in total levels of Tyr-phosphorylated proteins was detected by immunoblotting using a pan phospho-tyrosine antibody although there was also evidence of increased p-Y of some proteins (*) (FIG. 12). Importantly, both [L.sub.2Cu.sub.3].sup.6+ and [L.sub.2Zn.sub.3].sup.6+ treatment resulted in increased levels of the p53 tumour suppressor protein which is induced by many different types of cellular stress resulting in the co-ordination of an appropriate stress response which can include cell cycle arrest or cell death induction..sup.41 Whilst p53 levels were increased by ˜1.7 fold by [L.sub.2Cu.sub.3].sup.6+ and ˜2.7 fold by [L.sub.2Zn.sub.3].sup.6+ treatment in the HCT116 cancer cells, levels of p53 actually decreased with treatment in the ARPE19 non-cancer cells further indicating differential effects of the complexes on cancer versus non-cancer cells (FIG. 12). The earlier chemosensitivity results indicate, however, that the cytotoxicity of the [L.sub.2Cu.sub.3].sup.6+ and [L.sub.2Zn.sub.3].sup.6+ is not dependent on p53; indeed both complexes were more active towards the HCT116 p53.sup.−/− cells than the isogenic p53.sup.+/+ cells (FIG. 7a).

    Further Results

    [0664] Chemosensitivity studies results: The effect of anions on the potency and selectivity of all test compounds evaluated is presented in FIGS. 13-15. The inclusion of anions either increased, decreased or had no effect on both potency (FIG. 13) and the selectivity (FIG. 14) of [L.sub.2Cu.sub.3].sup.6+ and [L.sub.2Zn.sub.3].sup.6+. Enhanced or reduced effects on potency and selectivity relative to [L.sub.2Cu.sub.3].sup.6+ and [L.sub.2Zn.sub.3].sup.6+ was strongly cell line dependent (FIG. 15). Particularly marked enhancement of both potency and selectivity (relative to ARPE-19) was observed for PSN1 and HCT116 p53.sup.+/+ cells treated with Cu.sup.2+ and Zn.sup.2+ ligands plus sulfate and phenyl phosphate anions. In contrast, the potency of the Cu.sup.2+ ligand plus the phenyl phosphate anion against BxPC3 cells is significantly reduced resulting in a reduction in selectivity compared to ARPE-19 cells. Different effects on non-cancer cell lines were also observed with only marginal effects of anion inclusion observed for the Cu.sup.2+ ligand (against both ARPE-19 and MCF10A cells) whereas for the Zn.sup.2+ ligand, its activity in the presence of all the anions tested was significantly reduced resulting in a relative loss of selectivity (FIG. 15). This suggests that the activity and selectivity of complexes can be tailored to individual cell lines, possibly via modulation of specific kinase inhibition activity and cell line dependent susceptibility to subsequent effects on the kinome.

    [0665] Inhibition of kinase activity: The effect of [L.sub.2Cu.sub.3].sup.6+ and [L.sub.2Zn.sub.3].sup.6+ on the activity of 140 human recombinant kinases is presented in FIG. 16. Both compounds are multi-kinase inhibitors and visually, there are clear differences between the kinases that are inhibited by [L.sub.2Cu.sub.3].sup.6+ and [L.sub.2Zn.sub.3].sup.6+ with more [L.sub.2Cu.sub.3].sup.6+ inhibiting more kinases than [L.sub.2Zn.sub.3].sup.6+. The differences that exist indicate that a different spectrum of inhibitory activity exists with evidence of selectivity. Of interest, are the results demonstrating that the activity of some kinases is enhanced following drug treatment, particularly Src where significant stimulation of kinase activity was observed in these cell free assays.

    [0666] Autophagy studies: The effects of 3.125 μM [L.sub.2Cu.sub.3].sup.6+, [L.sub.2Zn.sub.3].sup.6+ and [L.sub.2Mn.sub.3].sup.6+ treatments (40 h) on the induction of cellular vacuoles and autophagy in the HCT116 p53.sup.−/−, HCT116 p53.sup.+/+ and ARPE19 cells are presented in FIGS. 17-19 with representative cell images shown. At this concentration, induction of autophagy was most pronounced in the HCT116 p53.sup.−/− cells with [L.sub.2Mn.sub.3].sup.6+ treatment followed by [L.sub.2Zn.sub.3].sup.6+ with no or little autophagy induced by [L.sub.2Cu.sub.3].sup.6+ compared to vehicle control treated cells (FIG. 17). In the HCT116 p53.sup.+/+ cells, induction of autophagy was also evident in the [L.sub.2Mn.sub.3].sup.6+ treated cells but was barely detectable in the [L.sub.2Zn.sub.3].sup.6+ treated cells at this concentration compared to in the HCT116 p53.sup.−/− cells (FIG. 18). This is consistent with [L.sub.2Zn.sub.3].sup.6+ being ˜6-fold more active towards the HCT116 p53.sup.−/− cells than the HCT116 p53.sup.+/+ cells based on 96 h IC.sub.50 values. In the ARPE19 cells, levels of autophagy were low with all treatments and similar to basal levels in control-treated cells (FIG. 19).

    [0667] Cellular ATP studies: The effects of 20 h treatment with a range of different concentrations of [L.sub.2Cu.sub.3].sup.6+, [L.sub.2Zn.sub.3].sup.6+ and [L.sub.2Mn.sub.3].sup.6+ on total cellular ATP levels in HCT116 p53.sup.+/+ and ARPE19 cells are presented in FIG. 20. Differential effects are observed depending on the metal in the complex, with [L.sub.2Mn.sub.3].sup.6+ having the most profound effects on both the HCT116 p53.sup.+/+ cancer and ARPE19 non-cancer cells. 6.25 μM [L.sub.2Mn.sub.3].sup.6+ treatment for 20 h reduced ATP levels in the HCT116 p53.sup.+/+ cancer cells to <50% with ATP levels declining less in the ARPE19 non-cancer cells but reaching ˜40% with 100 μM [L.sub.2Mn.sub.3].sup.6+ treatment. [L.sub.2Zn.sub.3].sup.6+ also reduced ATP levels in the HCT116 p53.sup.+/+ cancer cells with levels reduced to <50% at concentrations of ≥25 μM [L.sub.2Zn.sub.3].sup.6+ whereas in the ARPE19 cells ATP levels remained >70% with 100 μM [L.sub.2Zn.sub.3].sup.6 treatment. Effects of [L.sub.2Cu.sub.3].sup.6+ on ATP levels was much less, with ATP levels in the HCT116 cells reduced to <50% only at the highest concentration of 100 μM.

    SUMMARY

    [0668] In summary, in this study three different metal-containing, self-assembled anion binding complexes are characterised and shown to have distinctive chemical and biological properties. Depending on the metal, the reactivity of the complexes towards different anionic species varied with the Zn.sup.2+ and Mn.sup.2+ complexes both showing significant phosphatase activity but with different rates of hydrolysis (Mn.sup.2+>>Zn.sup.2+) whereas the Cu.sup.2+ complex bound to, rather than hydrolysed, phospho-containing species. Remarkable selective activity towards particular cancer cells compared to non-cancer cells was shown by the Zn.sup.2+ and Cu.sup.2+ complexes by different mechanisms with the modulation of multiple kinases via either binding (Cu.sup.2+) or by de-phosphorylation (Zn.sup.2+) of regulatory sites on kinases. Zn.sup.2+ and Mn.sup.2+ complexes both induced cancer cell autophagy consistent with cellular ATP deficiency and bioenergetic failure as a result of their phosphatase activity and futile cycles of re-phosphorylation by oncogenic kinases. Further modulation of activity and selectivity profile by incorporation of different anions (eg. PO.sub.4.sup.3−, SO.sub.4.sup.2− or PhOPO.sub.3.sup.2−) pre-cell exposure indicates the ease of generating numeromodular' combinations of metal/anion binding self-assembling complexes that can differ in potency, selectivity and mechanism(s) of action towards disease.

    PART B

    Overview

    [0669] [L.sub.2Cu.sub.3].sup.6+ and [L.sub.2Zn.sub.3].sup.6+ were evaluated at three different doses for in ovo anti-cancer activity, toxicity and anti-metastatic activity against tumors initiated from three different human cancer cell line models (H460, HT29, HCT116), in the chick embryo chorioallantoic membrane (CAM) assay.

    Methodology

    [0670] Each compound was provided to the contract research organisation (CRO) Inovotion (La Tronche, France) conducting the in ovo study, as a powder pre-weighed in single vials (2 equivalents of ligand, 3 equivalents of metal; and stored at room temperature). Before use, this was then dissolved in DMSO to 50 mM to generate a stock solution and further freshly diluted in RPM11640 or McCoys aqueous cell culture media for administration.

    [0671] A standard of care (SoC) drug for the particular tumour type was tested concurrently as a comparative control for in vivo efficacy and toxicity evaluation. A solvent control served as a negative control for both SoC and experimental compounds.

    [0672] 10.sup.6 tumor cells (H460, HT29 or HCT116) were grafted onto the upper chorioallantoic membrane (CAM) of the developing chick embryo on embryonic day 9 (E9). Access to the upper CAM was through a small hole drilled through the eggshell of fertilized White Leghorn eggs (into the air sac) on E9 (15 eggs per experimental group).

    [0673] 100 μl of freshly prepared experimental compound, vehicle control or standard-of-care (SoC) drug at their working concentrations were pipetted onto the tumor graft at E11, E13, E15 and E17. On day E18, the upper CAM (with tumor) was removed, washed by PBS buffer and then directly transferred in PFA (fixation for 48 hrs). After that, tumors were carefully cut away from normal CAM tissue and weighed.

    [0674] Embryonic viability was checked daily. The number of dead embryos was also counted on E18, to evaluate treatment-induced embryo toxicity.

    [0675] On day E18, a 1 cm.sup.2 portion of the lower CAM was collected (n=8 per group), stored at −20° C. and later processed to extract DNA. Samples were analysed for human genomic DNA (qPCR for Alu sequences) as a quantitative marker of tumor metastasis to the lower CAM.

    Results

    [0676] 1. In Vivo Efficacy Against Tumors Initiated from Human Lung Cancer Cell Line H460

    Reduction of H460 Tumor Growth

    [0677] Statistically significant regression of tumor growth (as determined by mean tumor weight at the end of the study, E18) was observed for [L.sub.2Zn.sub.3].sup.6+ at all three tested doses and for [L.sub.2Cu.sub.3].sup.6+ at the two highest tested doses (FIG. 21). Reduction of tumor growth for all three tested doses of [L.sub.2Zn.sub.3].sup.6+ and the highest dose of [L.sub.2Cu.sub.3].sup.6+ were comparable to that obtained with SoC.

    Analysis of Anti-Metastatic Activity

    [0678] Statistically significant decreases in H460 metastatic load were observed for all three doses of [L.sub.2Zn.sub.3].sup.6+ with reduction by the highest dose comparable to that observed with SoC (FIG. 22). However, there was no statistically significant metastatic regression with [L.sub.2Cu.sub.3].sup.6+ at the three tested doses indicating the differential effects of [L.sub.2Cu.sub.3].sup.6+ and [L.sub.2Zn.sub.3].sup.6+.

    Analysis of Embryonic Toxicity

    [0679] In term of toxicity, [L.sub.2Cu.sub.3].sup.6+ and [L.sub.2Zn.sub.3].sup.6+ were well tolerated at all doses tested with no statistically significant difference observed compared to the solvent (negative) control group (Table 1).

    TABLE-US-00001 TABLE 1 Percentage of alive and dead embryos per experimental group at the end of the H460 in ovo study. Group Gr. # Description Total Alive Dead % Alive % Dead 1 Neg. Ctrl. 14 12 2 85.71 14.29 2 SoC 14 12 2 85.71 14.29 3 L2Zn3 [1] 14 13 1 92.86 7.14 4 L2Zn3 [2] 13 10 3 76.92 23.08 5 L2Zn3 [3] 11 10 1 90.91 9.09 6 L2Cu3 [1] 14 12 2 85.71 14.29 7 L2Cu3 [2] 14 13 1 92.86 7.14 8 L2Cu3 [3] 14 12 2 85.71 14.29

    Summary (H460 Tumours)

    [0680] Overall, these results show that both [L.sub.2Cu.sub.3].sup.6+ and [L.sub.2Zn.sub.3].sup.6+ are well tolerated at all tested doses with [L.sub.2Zn.sub.3].sup.6+ shown to have comparable anti-cancer efficacy to the SoC in ovo, both in decreasing primary H460 tumor weight and metastatic burden. For [L.sub.2Cu.sub.3].sup.6+, at the highest dose tested, comparable anti-cancer activity to the SoC was also observed in decreasing H460 tumor weight, however, no statistically significant metastatic regression was observed.

    [0681] This provides the first evidence of in vivo efficacy of these compounds (at non-optimised doses) validating the anti-cancer activity and selectivity observed in vitro. The lack of embryonic toxicity observed suggests testing of higher doses is warranted (for potentially improved in vivo efficacy compared to the SoC).

    2. In Vivo Efficacy Against Tumors Initiated from Human Colon Cancer Cell Line HT29

    Reduction of HT29 Tumor Growth

    [0682] Statistically significant regression of tumor growth (as determined by mean tumor weight at the end of the study, E18) was observed for both [L.sub.2Zn.sub.3].sup.6+ and [L.sub.2Cu.sub.3].sup.6+ at their highest tested dose that was comparable that obtained with the SoC (FIG. 23).

    Analysis of Anti-Metastatic Activity

    [0683] There was no reduction in HT29 tumor cell metastasis to the lower CAM either with the SoC or any of the tested doses of [L2Cu.sub.3].sup.6+ and [L.sub.2Zn.sub.3].sup.6+ (data not shown).

    Analysis of Embryonic Toxicity

    [0684] [L.sub.2Cu.sub.3].sup.6+ and [L.sub.2Zn.sub.3].sup.6+ were well tolerated in the chick embryos grafted with HT29 colon cancer cells with increasing dose escalation showing no increased embryonic toxicity (Table 2).

    TABLE-US-00002 TABLE 2 Percentage of alive and dead embryos per experimental group at the end of the HT29 in ovo study. Group Gr. # Description Total Alive Dead % Alive % Dead 1 Neg. Ctrl. 15 14 1 93.33 6.67 2 SoC 14 14 0 100 0 3 L2Zn3 [1] 14 12 2 85.71 14.29 4 L2Zn3 [2] 14 13 1 92.86 7.14 5 L2Zn3 [3] 14 13 1 92.86 7.14 6 L2Cu3 [1] 14 10 4 71.43 28.57 7 L2Cu3 [2] 14 12 2 85.71 14.29 8 L2Cu3 [3] 13 12 1 92.31 7.69

    Summary (HT29 Tumours)

    [0685] Overall, these results show that both [L.sub.2Cu.sub.3].sup.6+ and [L.sub.2Zn.sub.3].sup.6+ are well tolerated at all tested doses with both [L.sub.2Cu.sub.3].sup.6+ and [L.sub.2Zn.sub.3].sup.6+ at the highest dose tested shown to decrease tumor weight to a similar level to that seen with the SoC. This provides further evidence of in vivo efficacy of these compounds (at non-optimised doses) against a second tumour type (colorectal cancer) and further validates the anti-cancer activity and selectivity observed in vitro. The lack of embryonic toxicity observed suggests testing of higher doses is warranted (for potentially improved in vivo efficacy compared to the SoC and anti-metastatic activity).

    3. In Vivo Efficacy Against Tumors Initiated from Human Colon Cancer Cell Line HCT116

    Reduction of HCT116 Tumor Growth

    [0686] Statistically significant regression of HCT116 tumor growth (as determined by mean tumor weight at the end of the study, E18) was observed for [L.sub.2Zn.sub.3].sup.6+ at the highest two doses tested and for [L.sub.2Cu.sub.3].sup.6+ at all three tested doses, although effects were not as pronounced as obtained with the SoC (FIG. 24).

    Analysis of Anti-Metastatic Activity

    [0687] Decreases in HCT116 metastatic load were observed for all three doses of [L.sub.2Zn.sub.3].sup.6+ comparable to that observed with SoC (FIG. 25).

    Analysis of Embryonic Toxicity

    [0688] In term of embryo toxicity, L2Zn3 and L2Cu3 were well tolerated at all doses tested with no statistically significant difference observed compared to the solvent (negative) control group (Table 3).

    TABLE-US-00003 TABLE 3 Percentage of alive and dead embryos per experimental group at the end of the HCT116 in ovo study. Group Gr. # Description Total Alive Dead % Alive % Dead 1 Neg. Ctrl. 17 15 2 88.24 11.76 2 SoC 15 14 1 93.33 6.67 3 L2Zn3 [1] 15 15 0 100 0 4 L2Zn3 [2] 15 13 2 86.67 13.33 5 L2Zn3 [3] 15 12 3 80.00 20.00 6 L2Cu3 [1] 14 14 0 100 0 7 L2Cu3 [2] 15 13 2 86.67 13.33 8 L2Cu3 [3] 15 13 2 86.67 13.33

    Summary (HCT116 Tumours)

    [0689] These results show that both [L.sub.2Cu.sub.3].sup.6+ and [L.sub.2Zn.sub.3].sup.6+ are well tolerated at all tested doses with [L.sub.2Zn.sub.3].sup.6+ at the highest two tested doses and for [L.sub.2Cu.sub.3].sup.6+ at all three doses resulting in statistically significant regression of tumor growth. In term of metastatic invasion, none of the conditions induce a significant regression of the metastatic load. However a strong regression tendency was observed for [L.sub.2Zn.sub.3].sup.6+ (all doses) similar to that obtained with the SoC. This provides further evidence of in vivo efficacy of these compounds (at non-optimised doses). The lack of embryonic toxicity observed suggests testing of higher doses is warranted (for potentially improved in vivo efficacy and anti-metastatic activity compared to the SoC).

    CONCLUSIONS

    [0690] [L.sub.2Cu.sub.3].sup.6+ and [L.sub.2Zn.sub.3].sup.6+ were both tested at three non-optimised doses (based on their in vitro IC.sub.50 values) for in vivo anti-cancer activity against tumors initiated from three different human cancer cell line models (H460, HT29, HCT116) in the chick embryo chorioallantoic membrane (CAM) assay. Against each tumour model, for both [L.sub.2Cu.sub.3].sup.6+ and [L.sub.2Zn.sub.3].sup.6+ statistically significant regression of tumour growth was observed, with effects most pronounced against the H460 lung cancer model (FIG. 21) and comparable to SoC for [L.sub.2Zn.sub.3].sup.6+ in both H460 and HT29 models (FIGS. 21, 23). Anti-metastatic effects were also observed for [L.sub.2Zn.sub.3].sup.6+ comparable to that obtained with the SoC in both H460 and HCT116 models (FIGS. 22, 25). Whilst these results provide initial proof-of-concept of in vivo anti-cancer efficacy with three different models to differing extents (most notably against the H460 lung cancer xenograft), it is also noteworthy that both [L.sub.2Cu.sub.3].sup.6+ and [L.sub.2Zn.sub.3].sup.6+ were extremely well tolerated (no statistically significant embryonic lethality) at the tested doses indicating scope for further dose escalation and optimisation.

    [0691] While specific embodiments of the invention have been described herein for the purpose of reference and illustration, various modifications will be apparent to a person skilled in the art without departing from the scope of the invention as defined by the appended claims.

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