METHOD OF PRODUCING METAL NANOPARTICLES AND USES THEREOF

Abstract

The invention disclosed herein relates to a method of producing metal particles of a preselected form in a biological system such a glycoprotein.

Claims

1. A method of producing metal particles of a preselected form, the method comprising reacting a combination of a glycoprotein or a complex of glycoprotein matrix and at least one a metal precursor with at least one a pH-adjusting agent, under conditions of at least pH permitting reductive transformation of said metal prec ursor to metal particles, wherein the pH-adjusting agent provides a pH between 3 and 9 and determines the fonn of the metal particle.

2. The method according to claim 1, wherein the metal particle provides a pH between 3 and 9 and is selected from particle size, shape and aggregation.

3. (caanceled)

4. The method according to claim 1, wherein the conditions permitting reductive transformation comprise selecting a reaction a temperature.

5. The method according to claim 1, wherein the pH is between 3 and 7, or between 3 and 6, or between 7 and 9.

6-7. (canceled)

8. The method of claim 4. wherein the conditions comprise reductive transformation at room temperature or at a temperature between 45 and 70° C.

9. The method according to claim 1, wherein the glycoprotein is at least one mucin.

10-11. (canceled)

12. The method according to claim 1. wherein the metal precursor is a metal salt or a metal complex.

13. The method according to claim 1, wherein the metal precursor comprises a metal atom selected from the group consisting of Ag, Au, Cu, Pd, Pt, Ni, Co, Cd, Fe, Sc, Sn, Al, Ti, V, Mn, Zn, Y, Zr, Nb, Tc, Ru, Rh, Mn, Hf, Ta, Re, In, Ga, Os, Ir, and any alloy thereof.

14-15. (canceled)

16. The method according to claim 12, wherein the metal precursor is a metal salt.

17-18. (canceled)

19. The method according to claim 1. wherein the pH-adjusting agent is selected from a group consisting of an acid or a base, a solution containing an acid or a base or a buffer solution of a specific pH.

20-21. (canceled)

22. The method according to claim 1, wherein the pH-adjusting agent is a borate buffer, the glycoprotein is porcine gastric mucin PGM), bovine submaxillary mucin (BSM or Q-mucin and the metal precursor is selected from the group consisting of silver, gold, and palladium metal precursor.

23. (canceled)

24. The method according to claim 1, wherein the metal particles are selected from the group consisting of nanoparticles, microparticles and a combination thereof.

25. The method according to claim 24, wherein the nanoparticles are of a size of between 20 and 50 mn.

26. The method according to claim 24. wherein the microparticles are of a size of between 1 and 5 microns.

27-30. (canceled)

31. The method according to claim 1. further comprising a step of separating the metal particles from the glycoprotein.

32. A method of synthesis of metal particles, the method comprising causing reduction of at least one metal precursor, under pH-dependent conditions, in a biological matrix comprising at least one glycoprotein, wherein the pH-dependent conditions affect at least one conformational change in the glycoprotein, to thereby control the particles shape, size and aggregation.

33. A method of producing metal particles, the method comprising affecting a change in a conformational state of at least one glycoprotein enriched with a metal precursor by adjusting/altering the pH of the at least one glycoprotein, thereby causing reduction of the metal precursor to a metal particle.

34. (canceled)

35. A glycoprotein/metal particle complex obtained according to a method of claim 1.

36. A glycoprotein/metal particle complex comprising: Q-mucin and a population of gold particles, wherein the particles are of a size ranging between 0.5 μm and 1.5 μm and/or between 10 nm and 100 nm; or PGM and a population of gold particles, wherein the particles are of a size ranging between 0.5 μm and 1.5 μm and/or between 10 nm and 100 nm in size.

37. A film comprising a glycoprotein/metal particle complex accor ding to claim 35 or 36.

38. A method for treating water comprising contacting water to be treated with a glycoprotein/metal particle complex according to claim 35.

39. A method of antibacterial treatment comprising contacting a surface to be treated with a glycoprotein/metal particle complex according to claim 35.

40. (canceled)

41. A method for treating water comprising contacting with water to be treated and a catalyst comprising a glycoprotein/metal particle complex according to claim 35.

Description

BRIEF DESCRIPTION OF THE DRAWINGS

[0153] In order to better understand the subject matter that is disclosed herein and to exemplify how it may be carried out in practice, embodiments will now be described, by way of non-limiting example only, with reference to the accompanying drawings, in which:

[0154] FIGS. 1A-D depict: FIG. 1A—main structural components of PGM proteins. FIG. 1B—PGM protein schematic structure. FIG. 1C—PGM unfolded structure under acidic pH. FIG. 1D—PGM folded structure under alkaline pH.

[0155] FIGS. 2A-G provide a schematic representation of the proposed mechanism of gold particles formation in PGM glycoprotein. FIG. 2A—PGM structure in neutral pH, FIG. 2B—PGM structure in neutral pH after addition of gold ions, FIG. 2C—PGM-gold complex in acidic pH, FIG. 2D—PGM-gold complex in alkaline pH, FIG. 2E—Gold nanoparticles formed in acidic pH, FIG. 2F—Gold nanoparticles formed in alkaline pH, FIG. 2G—PGM structure schematic.

[0156] FIGS. 3A-B provide: FIG. 3A—PGM-Gold nanoparticles complex solutions in different pH buffers, from left to right pH3, pH6 and pH9, FIG. 3B—Marine mucine-Gold nanoparticles complex solutions in different pH buffers, from left to right pH3,pH6 and pH9.

[0157] FIG. 4 provides UV-Vis absorption spectra for samples of PGM-AuNp complex in X-6=pH3, X-7=pH6, and X-8=pH9 in water from 250 840 nm.

[0158] FIGS. 5A-B present (FIG. 5A) Gold nano triangle synthesized by PGM and its energy-dispersive X-ray spectrum (FIG. 5B).

[0159] FIGS. 6A-F depict PGM glycoprotein-AuNp complex in different pH environments. FIG. 6A and FIG. 6B—PGM-AuNp complex in pH=3, FIG. 6C and FIG. 6D—PGM-AuNp complex in pH=6, FIG. 6E and FIG. 6F—PGM-AuNp complex in pH=9.

[0160] FIGS. 7A-F depict marine mucin glycoprotein (M-mucin)-AuNp complex in different pH environments. FIG. 7A and FIG. 7B- M-mucin-AuNp complex in pH=3, FIG. 7C and FIG. 7D—M-mucin-AuNp complex in pH=6, FIG. 7E and FIG. 7F—Q-mucin-AuNp complex in pH=9.

[0161] FIGS. 8A-F depict the synthesis of gold nanoparticles on M-mucin solid films in different pH environments. FIG. 8A and FIG. 8B—M-mucin film -AuNp complex in pH=3, FIG. 8C and FIG. 8D—M-mucin film-AuNp complex in pH=6, FIG. 8E and FIG. 8F—M-mucin film-AuNp complex in pH=9.

[0162] FIGS. 9A-D depict the synthesis of gold nanoparticles on M-mucin nanofibers in pH=3. FIG. 9A and FIG. 9B—M-mucin nanofibers scaffold with dipped into M-mucin-AuNp complex pH=3, FIG. 9C and FIG. 9D—synthesis of AuNp on M-mucin nanofibers in pH=3.

[0163] FIG. 10 provides temperature measurements of solutions containing samples of PGM+AuNp XL3-XL4 (pH9) and XL5-XL8 (pH3) as a function of irradiation time using a NIR laser at 808 nm and 1.25 W/cm3. Samples were irradiated for 50, 100, and 200 seconds from room temperature. Measurements were carried out in triplicates (n=3).

[0164] FIG. 11 provides temperature measurements of irradiation by NIR laser at 808 nm and 1.25W/cm3 of solid film of X-6 sample dried on glass slide.

[0165] FIG. 12 provides water condensation under irradiation of 808 nm laser.

[0166] FIG. 13 provides weight loss vs. time of DI reference and PGM-AuNp samples (XL8, XL8 sponge, LS.sub.3, NF LS.sub.3).

[0167] FIG. 14 A-B provides water evaporation rate in the presence and absence of gold nanoparticles. FIG. 14A—under solar simulator (1kW/m.sup.2): water mass as a function of time. Yellow line-pH7, red line-water only, green: pH4, 30 mg, blue: pH4, 70C. FIG. 14B—under sun light: blue: only water, green: pH7, orange: pH4, 30 mg, dark green: pH4, 70° C.

[0168] FIG. 15A-C depict the synthesis of gold nanoparticles in PGM under various pH conditions. FIG. 15A—image of the solutions in the pH range of 2-10 (increase in pH from left to right). FIG. 15B—UV-vis spectra of the PGM+AuNp complexes at the different pH (2-10). FIG. 15C—temperature measurements of solutions containing samples of PGM+AuNp at pH 2-10 as a function of the pH using a NIR laser at 808 nm and 4W after 10 min of irradiation.

[0169] FIG. 16A-C depict the synthesis of gold nanoparticles in different PGM mass (10-90 mg). FIG. 16A—image of the solutions PGM mass increases from left to right. FIG. 16B—UV-vis spectra of the PGM+AuNp complexes at the different PGM mass. FIG. 16C—temperature measurements of solutions containing samples of PGM+AuNp in different PGM mass as a function of the pH using a NIR laser at 808 nm and 4W after 10min of irradiation.

[0170] FIG. 17A-C depict the synthesis of gold nanoparticles in PGM at different Au concentrations. FIG. 17A—image of the solutions [Au] increases from left to right. FIG. 17B—UV-vis spectra of the PGM+AuNp complexes at different Au concentrations. FIG. 17C—temperature measurements of solutions containing samples of PGM+AuNp at different Au concentrations as a function of the pH using a NIR laser at 808 nm and 4W after 10min of irradiation.

DETAILED DESCRIPTION OF EMBODIMENTS

[0171] FIG. 1 provides depiction of mucin conformational forms. The pH depended formation of various gold nanoparticles structures in PGM protein matrix may be explained by the mechanism show in FIG. 2. The reducing active group of mucin glycoprotein mainly located in the hydrophobic regions along the main protein chain. Those hydrophobic domains mainly consist from cysteine amino acids with active thiols groups (FIG. 2G). During the exposure of mucin protein to protons or hydroxyls the protein changes its configuration by exposing the hydrophobic regions (acidic conditions) (FIG. 2C) or on the contrary keeping them closed with stabilized salt bridges between negative and positive charged amino acids (alkaline conditions) (FIG. 2D). The exposure of the hydrophobic regions allows hydrophobic interactions between mucin individual proteins leading to formation of dense gel networks of mucin units. On the other hands when the hydrophobic regions are closed the mucin protein sub units interact with each other only via electrostatic level leading to loose structure with considerably larger space between the individual mucin units. When the gold ions are mixed with mucin glycoprotein in neutral pH (FIG. 2B) they are entering the hydrophobic domains and begin the nucleation process forming the gold seeds which act as precursor for future nanoparticles. With addition of protons the hydrophobic domains are opening allowing hydrophobic interactions between the mucin units. This promotes contact between the gold seeds located in diverse mucin units by this allowing formation of hexagonal and trigonal particles in newly formed hydrophobic domains (FIG. 2E) and circular particles (FIG. 2F) in closed hydrophobic domains. Addition of hydroxyls promotes repulsion of the mucin units by electrostatic forces by this maintaining the hydrophobic domains enclosed limiting the interaction between them. Those limited protein interactions promotes formation of dispersed circular nanoparticles.

[0172] Apparently the pH conditions effect not only the PGM conformation but also the reduction reaction kinetics. In alkaline conditions the reduction reaction proceeds in much faster rate than in acidic pH. This may be explained by the close proximity of thiol units in closed hydrophobic domains to the gold seeds which induces the reduction process and buildup of the gold circular nanoparticles. In acidic pH the distance between the thiols is larger by this allowing slower buildup of gold particles by this allowing formation of more complex hexagon and triangular nanostructures and microstructures.

[0173] Example of Process Including Materials, Process and Results:

[0174] Materials:

[0175] In the present invention the next materials were used:

[0176] AgNO3 (sigma), HAuClH4 (sigma), NaAuClH4(sigma), PdCl2 (sigma), Porcine Gastric Mucin (PGM) (sigma), Marine Mucin, Hydrochloric acid (sigma), Sodium Hydroxide (sigma), Glycine(sigma), Ethanol anhydrous (Merck), Aqua regia, PCL(sigma)

[0177] Synthesis of Ag Nanoparticles—XJF, PGM sol

[0178] Typical synthesis of Ag nanoparticles in mucin protein matrix involves the next steps:

[0179] Appropriate Mucin protein (M-Qmucin/PGM) is weighted with typical protein weight is between 10-50 mg in lyophilized form or 0.5-1 gram in non-lyophilized form. The mucin protein is dissolved in 3 ml of AgNO.sub.3 solution that can be between 2.5*10.sup.−5 M to 2.5*10.sup.−3 M. After lhr of stirring borate buffer of pH=9 is added to the Mucin-Ag+ solution. The Mucin-Ag+ solution is left for stirring in dark till completion of the reaction. Typical synthesis time is between 48-72 hr depending on silver salt concentration and on mucin type.

[0180] Synthesis of Au Nanoparticles—M-Qmucin, PGM sol

[0181] Appropriate Mucin protein (M-Qmucin/PGM) is weighted with typical protein weight is between 10-50 mg in lyophilized form or 0.5-1 gram in non-lyophilized form. The mucin protein is dissolved in AuClH.sub.4 solution which volume can 2.5 ml to 5 ml that can be between 2.5*10.sup.−5 M to 2.5*10.sup.−3 M and stirred for lhr. To the previously dissolved Mucin protein-gold ions solution we add Glycine buffer in volume that can be between 2.5 ml-5 ml with appropriate pH value (3, 6, 9). After the addition of appropriate buffer the complex solution is purged from oxygen by addition of ambient nitrogen gas and sealed with parafilm. The reaction solution is stirred in dark in 45 degrees for 48 hr-72 hr till appropriate color appears (FIGS. 3A and 3B). Glycine buffer pH is responsible for Mucin conformational changes which have direct effect on synthesized gold nanoparticles size, shape, diffraction and optical properties (FIG. 4). Mucin-Au+complex in glycine buffer of pH=3 results in synthesis of mostly triangular (FIG. 5) and hexagonal particles (FIG. 6A and 6B) with size range between 0.5 μm-1.5 μm and circular dispersed nanoparticles with size range between 10 nm-100 nm. Mucin-Au+complex in glycine buffer pH=6 results in circular nanoparticles with mild aggregation and size range between 20 nm-50 nm (FIG. 6C and 6D). Mucin-Au+ complex in glycine buffer pH=9 results in circular nanoparticles in heavy aggregative state and size range 20 nm-50 nm (FIG. 6E and 6F).

[0182] Similar HR-TEM observations were made in synthesis of Au nanoparticles in M-Qmucin proteins (FIG. 7).

[0183] Synthesis of Au Nanoparticles Mucin Solid Film

[0184] Typical synthesis of Au nanoparticles on mucin solid protein film involves two preparative steps. First the mucin solid protein film is prepared by drying the M-Qmucin protein gel/paste under fume hood or vacuum until formation of solid uniform film.

[0185] Second the mucin solid protein film with typical minimum weight of 50-100 mg is added to AuClH.sub.4 solution of 2.5*10.sup.−5 M to 2.5*10.sup.−3M and stirred till gold ions are absorbed into the film (1-2 hr). After the Au ions absorbance into the film, 3 ml of glycine buffer is added in pH values 3-9 in order to synthesize Au nanoparticles with different shapes as previously described (FIG. 8). After stirring the mucin film-Au complex for 48 hr in RT the film can be dried under fume hood or solubilized in heated strong acid for example 1M HCl or Acetic acid.

[0186] Synthesis of Au/Ag Nanoparticles on Mucin Nanofibers

[0187] Typical synthesis of Au nanoparticles on Mucin nanofibers involves two primary steps:

[0188] First is the Mucin nanofibers preparation and second synthesis of Au or Ag nanoparticles on the structural matrix of Mucin nanofibers.

[0189] In order to prepare Mucin nanofibers, 50 mg of pristine Mucin protein or mixture of Mucin protein and other bio polymers such as collagen, hyaluronic acid, cellulose, gelatin are added to a carrier solvent that can be acetic acid, aqua regia, HFIP, TFA, acetic acid/ethanol, acetic acid/chloroform and others and stirred until full solubilization.

[0190] After the solubilization of the mucin proteins the stabilizing co-polymer is added in appropriate ratio to the protein that can be from 10%/90% co-polymer/protein mass to 50%/50% co-polymer/protein mass and stirred till full solubilization of the co-polymer in the carrier solvent.

[0191] The co-polymers that can be used in the process of the formation of the mucin nanofibers are: poly-caprolactone (PCL), poly vinyl alcohol (PVA), poly-lactic acid (PLA), sodium alginate, poly styrene and others.

[0192] The mucin protein-co polymer complex solution is then loaded into electrospinning setup and ran under various electrospinning conditions such as electrode distance, solution flow speed and applied voltage. The electrospinning conditions also heavily depend on the co-polymer type. Typical electrospinning conditions for an example with co-polymer PCL include: flow speed: 3 microliter/minute, electrode distance: 24 cm, voltage:14 kV. The average diameter of the formed Mucin nanofibers is 200-300 nm with porosity of 25%-35%.

[0193] The second step is synthesis of metal nanoparticle on the nanofibrous matrix of Mucin nanofibers. In typical synthesis procedure, the mucin nanofiber scaffold is cut into rectangular scaffolds of 2×2 cm and washed with DI in order to remove any residual solvent traces. Afterwards the mucin scaffolds are put into 2 ml Au ions and 3 ml of appropriate buffer OH solution and stirred for 24 hr in dark.

[0194] The shape and size of the nanoparticles (FIG. 9) have clear indication of pH dependency as in gold nanoparticles synthesis in solution. Mucin nanofibers and gold ions in acidic conditions lead to synthesis of triangular and hexagonal nanoparticles. synthesis in neutral and alkaline pH leads to creation of circular gold nanoparticles concentrated in aggregates and spread on nanofibers surface.

[0195] Synthesis of Pd Nanoparticles in Mucin Protein

[0196] Typical synthesis of Pd nanoparticles in mucin protein matrix involves the next steps: Appropriate Mucin protein is weighted with typical protein weight is between 10-50 mg in lyophilized form, or 0.5-1 gram in non-lyophilized form. The mucin protein is dissolved in 3 ml of PdCl.sub.2 solution that can be between 2.5*10.sup.−5 M to 2.5*10.sup.−3 M. After lhr of stirring borate buffer of pH=9 is added to the Mucin-Pd+solution. The Mucin-Pd+ solution is left for stirring in dark till completion of the reaction. Typical synthesis time is between 48-72 hr depending on Palladium salt concentration and on mucin type.

[0197] Synthesis of Alloy Nanoparticles in Mucin: Pd—Au, Pd—Ag, Au—Ag

[0198] Synthesis of alloy nanoparticles of Pd—Au, Pd—Ag, Au—Ag in mucin proteins follows the same synthesis protocol of stand-alone synthesis of metal nanoparticle in mucin with several additional steps. After completion of synthesis of Au/Ag/Pd Np in mucin protein in order to synthesizes desired alloy nanoparticle we add 1 ml of 2.5*10.sup.−31 3 of Ag/Au/Pd metal ion solution. The complex solution is stirred in RT for 48 hr until completion of the reaction.

[0199] Optical and Hyperthermia Measurements of Au Nanoparticles Synthesized By Mucin Proteins

[0200] Samples of PGM+Au nanoparticles in different pH conditions X-6=pH3, X-7=pH6, and X-8=pH9 were prepared at a concentration of 1.7 mM Au in deionized water. In order to determine their optical properties, sample solutions were diluted by a factor of 10, and placed in plastic cuvettes with a beam path length of 10 mm UV-Vis spectra were recorded accordingly in a Nanodrop™2000c fitted with a cuvette reader (Thermo Scientific, Australia). The spectra for each sample were measured from 250 to 840 nm (FIG. 4).

[0201] From FIG. 4 it may be concluded that each of the samples exhibited strong absorption at 280 nm, usually associated with aromatic rings in tyrosine and tryptophan amino acids comprising the surface protein layer. Additionally, broad peaks centered around 580 nm for X-7 and X-8 were associated with plasmon resonance effects originating from the 20 nm Au nanoparticles, while no such peak was observed for the sample X-6. Finally, absorption at 808 nm was much more intense for X-6 as opposed to samples X-7 and X-8.

[0202] The samples were then irradiated with an 808 nm continuous wave diode laser at a power density of 1.25 W/cm.sup.3 in water for 50, 100, and 200 sec (FIG. 10). The temperature of the solutions was measured pre- and post-irradiation using a FLIR (i7) thermo-imaging camera (n=3). Results showed a drastic increase in temperature for XL-5,XL-6,XL-7 and XL-8 after irradiation for 50 sec from room temperature to 90-100° C. and maximum of 120° C. after 200 sec. Heating effect was less drastic for XL-3 and XL-4 which temperature increase was measured at 40° C. for XL-3 and 60° C. for XL-4 after 50 sec and reached a maximum temperature of 58° C. and 90° C. for XL-3 and XL-4 respectfully. The higher heating effect value was attributed to the enhanced absorption of XL-5 . . . XL-8 samples in the NIR region of the spectrum (800 1200) as is shown in FIG. 10. Given that the [Au]=1.7 mM for all samples, the difference in NIR absorption was attributed purely to particle geometry, shape, and size.

[0203] Samples of PGM+Au nanoparticles in different pH conditions, Au concentration, and PGM mass were used for optimization of the hyperthermia effect under laser 808 nm irradiation. The solution that provide the most drastic heating effect will be considered as the optimized synthesis procedure. In order to determine their optical properties, samples were diluted and placed in plastic cuvettes with a beam path length of 10 mm UV-Vis spectrums were recorded as previously described. The spectra for each sample was measured from 300 to 1000 nm. The samples were irradiated with an 808 nm continuous wave diode laser at a power density of 4 W in water for 10min The temperature of the solutions was measured pre- and post-irradiation using a thermocouple.

[0204] Solutions with pH 2-10 were prepared at a concentration of [Au]=1.25 mM in deionized water (FIG. 15A). The samples under pH conditions of pH=9, 10 exhibited strong absorption centered around 550 nm, whereas pH=2, 3, 7, 8 exhibited a broad weak peak centered around 550 nm associated with plasmon resonance effects. The differences in the intensity of the peaks is associated with the particles average size, which is smaller for the particles with the broad and weaker peaks. No such peak was observed for the samples pH=4, 5, 6 (FIG. 15B). Finally, heating effect at 808 nm was the most intense for pH=4, 6 (FIG. 15C).

[0205] Later, a range of PGM mass (10-90 mg) with an identical amount of water at pH=4 and [Au]=1.25 mM were prepared (FIG. 16A). The sample of pH4 with 30 mg of PGM exhibited strong absorption centered around 550 nm, 70 mg and 10 mg of PGM exhibited a broad weak peak centered around 550 nm associated with plasmon resonance effects, whereas no peak was excepted for 50 mg and 90 mg of PGM (FIG. 16B). Finally, heating effect at 808 nm was the most intense for pH4, 50 mg of PGM (FIG. 16C).

[0206] Finally, a range of Au concentrations, 0.42-1.56 mM, with 50 mg PGM at pH=4 and [Au]=1.25 mM were prepared (FIG. 17A). The samples of pH4 with 4-5m1 of Au (1.43 and 1.56 respectively) exhibited strong absorption centered around 550 nm, whereas no peak was excepted for the three lower concentrations (FIG. 17B). Finally, heating effect at 808 nm was the most intense for [Au]=1.25 mM (FIG. 17C).

[0207] Additional hyperthermia measurement experiment in solid state was performed on sample XL-3 which was dried on an glass slide. The experiment showed that in solid state the X-6 can go through several cycles of heating without any damage to the protein sample (FIG. 11).

[0208] Water Condensation Experiments Under Laser Irradiation (808 nm)

[0209] Samples with PGM-gold Np complex were put in DI in 5%/95% (PGM/DI) ratio and irradiated for duration of 15 minutes by 808 nm NIR laser.

[0210] Before, during and after the laser treatments both PGM-AuNp and DI reference were weighted and the mass loss to water condensation was calculated (FIG. 12). From the experimental results we calculated that the water condensation of PGM-AuNp samples was higher by 30% then in referenced DI sample.

[0211] Water Condensation Under Solar Lamp

[0212] Several samples of PGM-AuNp complexes diluted in DI water or inserted into carrier membrane were put under solar simulator (450W, 1.5 AM) and irradiated with solar light for different time durations (30sec, 45 sec, 60 sec, 120 sec and 300 sec). PGM-AuNp and DI reference were weighted before and after solar irradiation and the mass loss to water condensation was calculated (FIG. 13). From the experimental results we calculated that the water condensation of PGM-AuNp samples(XL8,XL8 sponge, LS.sub.3 and NF LS.sub.3) was higher by 20%-92% then in referenced DI sample depending on PGM-AuNp type and concentration (Table 1).

TABLE-US-00001 TABLE 1 Weight loss under solar irradiation DI XL8 Time (sec) water XL8 sponge LS3 NF LS3 0 0 0 0 0 0 30 −0.0039 −0.008 −0.0092 −0.0178 −0.0063 45 −0.0047 −0.0043 −0.0038 −0.0035 −0.0056 60 −0.0049 −0.0064 −0.0067 −0.0068 −0.0075 120 −0.0089 −0.0124 −0.0091 −0.0103 −0.0067 300 −0.0133 −0.0195 −0.0139 −0.0305 −0.0174 Weight loss (gr) 0.0357 0.0506 0.0427 0.0689 0.0435 after total 9 minutes

TABLE-US-00002 TABLE 2 exemplary systems prepared according to methods of the invention Mucin Resulting glycoprotein Metal Buffer pH particle size Resulting shape M-Qmucin Ag Borate 9 PGM Ag Borate 9 M-Qmucin Au Glycine 3 0.5 μm-1.5 μm triangular and hexagonal particles  10 nm-100 nm circular dispersed nanoparticles M-Qmucin Au Glycine 6 20 nm-50 nm circular nanoparticles with mild aggregation M-Qmucin Au Glycine 9 20 nm-50 nm circular nanoparticles in heavy aggregative state PGM Au Glycine 3 0.5 μm-1.5 μm triangular and hexagonal  10 nm-100 nm particles (Additional comments: (1) Enhance NIR absorption comparable to NP at PH = 6 and PH = 9. (2) undergo several cycles of heating without damaging the protein sample. (3) No cytotoxicity in cancer cells. (4) Enhanced water condensation under laser irradiation. (5) Enhanced water condensation under solar lamp). (6) circular dispersed nanoparticles Able to PGM Au Glycine 6 20 nm-50 nm circular nanoparticles with mild aggregation PGM Au Glycine 9 20 nm-50 nm circular nanoparticles in heavy aggregative state PGM Pd borate 9  5-20 nm Circular PGM *Pd—Au *Borate and glycine 9 to 3 *5-100 nm  *Circular *Pd—Ag *Borate 9 and 9 *5-20 nm *Circular *Au—Ag *glycine and borate 3 to 9 *0.5 μm-1.5 μm *Triangular and circular and 5-20 nm (Additional comments: Au—Ag antibacterial material with anti- biofilm capabilities)

[0213] Water Evaporation Rate in Solar Simulator and Field Test Several samples of PGM-AuNp complexes were examined under solar simulator (1kW/ m.sup.2) and in field test under the sun. The solutions were diluted in DI water to identical concentration and weigh on a scale in fixed time periods for measuring water loss rate of each solution. The experiment was performed 5 times for statistics. The same samples were also examined in field tests. The experiment was performed 5 times for statistics (FIG. 14). The experimental results revealed a significant increase in the efficiency of photothermal energy conversion-reaching up to 0.80 Kg/m.sup.2h water loss under 1 sun (1kW/ m.sup.2) for particles solution in water, compared to about 0.34 Kg/m.sup.2h water loss for a system consisted only of water (Table 3).

TABLE-US-00003 TABLE 3 Water weight loss under solar irradiation Water loss water loss rate [Kg/hr*m.sup.2] solar simulator field test 0.796 y = −0.0211x + 6.676  y = −1.9961x + 6.6559 pH 7, 3:3 0.74 y = −0.0257x + 6.7913 y = −1.9869x + 7.0016 pH 4, 30 mg 0.736 y = −0.0274x + 6.7399 y = −2.0734x + 6.5736 pH 4, 70° C. 0.337 y = −0.0188x + 6.7378 y = −1.8437x + 6.5298 H.sub.2O