A method of preparing a .sup.64Cu-BaBaSar-RGD.sub.2 solution is provided. The method includes lyophilizing a solution of BaBaSar-RGD.sub.2 and adding a .sup.64Cu solution to the lyophilized BaBaSar-RGD.sub.2.

Disclosed herein are methods preparing a purified, carrier-free 68Ga solution. Tire present disclosure also provides systems for preparing a purified, carrier-free 68Ga solution. The present disclosure also provides compositions comprising the purified, carrier-free 68Ga solutions disclosed herein. Also provided are methods of administering compositions of the present disclosure to a patient in need thereof, for example, for imaging a disease or disorder, such as cancer.

The present invention relates to compounds that are useful as metal ligands and which either contain a molecular recognition moiety or can be bound to a molecular recognition moiety and methods of making these compounds. Once the compounds that contain a molecular recognition moiety are coordinated with a suitable metallic radionuclide, the coordinated compounds are useful as radiopharmaceuticals in the areas of radiotherapy and diagnostic imaging. The invention therefore also relates to methods of diagnosis and therapy utilising the radiolabelled compounds of the invention.

The invention provides a radiopharmaceutical compound or composition comprising a radiolabeled linear peptide that binds specifically to Glypican-3 (GPC3) expressed on a surface of a cell. Preferably, the linear peptide is conjugated to one or more .sup.18F atoms.

The present invention provides peptides and peptide-conjugates that bind to α.sub.vβ.sub.6 integrin. The peptide-conjugates can be used for a variety of imaging and therapeutic applications. Methods of use and peptide optimization are also provided herein.

The present invention relates to a labeling procedure for the incorporation, in mild reaction conditions, of sensitive and thermosensitive targeting molecules into a [99m Tc(N)(PNP)]-based compound suitable for a kit formulation.

Compounds are described having albumin binding groups, where said compounds can be complexed with therapeutic and/or diagnostic agents and further can include targeting functionality. When introduced into the circulatory system the compounds and complexes bind serum albumin, and thereby exhibit useful properties including enhanced circulatory half-life, improved uptake by target tissues, and improved target/nontarget ratios. These properties make the compounds and complexes useful in therapeutic and diagnostic methods.

A method for preparing a complex comprising a radioisotope of gallium for use in radiotherapy or in a medical imaging procedure, said method comprising adding a gallium radioisotope solution obtained directly from a gallium radionuclide generator to a composition comprising a pharmaceutically acceptable buffer and optionally also a pharmaceutically acceptable basic reagent, in amounts sufficient to increase the pH to a level in the range of 3 to 8, wherein the composition further comprises a chelator that is able to chelate radioactive gallium within said pH range and at moderate temperature, said chelator being optionally linked to a biological targeting agent. Kits and compositions for use in the method are also described and claimed.

Engineered peptides that bind with high affinity (low equilibrium dissociation constant (Kd)) to the cell surface receptors of fibronectin (α.sub.5β.sub.1) or vitronectin (α.sub.vβ.sub.3 and α.sub.vβ.sub.5 integrins) are disclosed as useful as imaging tissue. These peptides are based on a molecular scaffold into which a subsequence containing the RGD integrin-binding motif has been inserted. The subsequence (RGD mimic) comprises about 9-13 amino acids, and the RGD contained within the subsequence can be flanked by a variety of amino acids, the sequence of which was determined by sequential rounds of selection (in vitro evolution). The molecular scaffold is preferably based on a knottin, e.g., EETI (Trypsin inhibitor 2 (Trypsin inhibitor II) (EETI-II) [Ecballium elaterium (Jumping cucumber)], AgRP (Agouti-related protein), and Agatoxin IVB, which peptides have a rigidly defined three-dimensional conformation. It is demonstrated that EETI tolerates mutations in other loops and that the present peptides may be used as imaging agents.

A method for removing or controlling or quantifying the presence of aldehydes, in particular acetaldehyde, is described. Such a method is useful in prolonging the shelf life of a pharmaceutical product.