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 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.

Scintillant-doped polystyrene core nanoparticles surrounded by a silica shell can be used to quantify low-energy radionuclides. The nanoparticles are recoverable and re-useable, which may reduce waste and allow for sample recovery. Unlike traditional liquid scintillation cocktail (LSC) formulations, the nanoparticles are made from non-toxic and non-volatile components, and can be used without the aid of surfactants, making them a possible alternative to LSC for reducing the environmental impact of studies that employ radioactive tracers. Recognition elements attached to the functionalized silica surfaces of the nanoparticles allow for separation-free scintillation proximity assay (SPA) applications in aqueous samples. Lipid membrane coatings deposited on the nanoparticle surface can significantly reduce the non-specific adsorption of proteins and other biomolecules, and allow for the incorporation of membrane proteins or other membrane associated binding molecules.

A noninvasive detection method for cancer metastases is provided, which are based on the feature of the radiopharmaceutical that binds specifically to cells of cancer hepatic metastasis, so that cancer metastases can be detected by detecting the signal of the radiopharmaceutical in various organs in the subject. A specific treating method for cancer metastases by using the radiopharmaceutical as an important tool for precise treatment is also provided.

A noninvasive detection method for cancer metastases is provided, which are based on the feature of the radiopharmaceutical that binds specifically to cells of cancer hepatic metastasis, so that cancer metastases can be detected by detecting the signal of the radiopharmaceutical in various organs in the subject. A specific treating method for cancer metastases by using the radiopharmaceutical as an important tool for precise treatment is also provided.

New chelators such as H.sub.3L1, H.sub.3L2, H.sub.3L3, H.sub.3L26 and derivatives were synthesized for the complexation of {Al.sup.18F}.sup.2+. These new chelators are able to complex {AI.sup.18F}.sup.2+ with good radiochemical yields using a labeling temperature of 37° C. The stability of the new Al.sup.18F-complexes was tested in phosphate buffered saline (PBS) at pH 7 and in rat serum. AI.sup.18F-L3 and AI.sup.18F-L26 showed a stability comparable to that of the previously reported Al.sup.18F-NODA. Moreover, the biodistribution of Al.sup.18F-L3 and AI.sup.18F-L26 showed absence of in vivo demetallation since only very limited bone uptake was observed, whereas the major fraction of activity 60 min p.i. was observed in liver and intestine due to hepatobiliary clearance of the radiolabeled ligand. The chelators H.sub.3L3 and Al.sup.18F-L26 demonstrated to be a good lead candidates for the labeling of heat sensitive biomolecules with .sup.18F-fluorine and derivatives have been synthesized. We have explored the complexation of {AI.sup.18F}.sup.2+ with new chelators and obtained very favourable radiochemical yields (>85%) using a labeling temperature of 37° C. The stability of the new Al.sup.18F-complexes was tested in phosphate buffered saline (PBS) at pH 7 and in rat serum at 37° C., where AI.sup.18F-L3 and AI.sup.18F-L26 showed a stability comparable to that of the previously reported Al.sup.18F-NODA. Moreover, the biodistribution of Al.sup.18F-L3 and Al.sup.18F-L26 showed high stability, since only very limited bone uptake—which would be an indication of release of fluorine-18 in the form of fluoride—was observed, whereas the major fraction of activity 60 min p.i. was observed in liver and intestines due to hepatobiliary clearance of the radiolabeled ligand. The chelators H.sub.3L3 and H.sub.3L26 demonstrated to be good lead candidates for the labeling of heat sensitive biomolecules with .sup.18F-fluorine and several derivatives have been synthesized.

New chelators such as H.sub.3L1, H.sub.3L2, H.sub.3L3, H.sub.3L26 and derivatives were synthesized for the complexation of {Al.sup.18F}.sup.2+. These new chelators are able to complex {AI.sup.18F}.sup.2+ with good radiochemical yields using a labeling temperature of 37° C. The stability of the new Al.sup.18F-complexes was tested in phosphate buffered saline (PBS) at pH 7 and in rat serum. AI.sup.18F-L3 and AI.sup.18F-L26 showed a stability comparable to that of the previously reported Al.sup.18F-NODA. Moreover, the biodistribution of Al.sup.18F-L3 and AI.sup.18F-L26 showed absence of in vivo demetallation since only very limited bone uptake was observed, whereas the major fraction of activity 60 min p.i. was observed in liver and intestine due to hepatobiliary clearance of the radiolabeled ligand. The chelators H.sub.3L3 and Al.sup.18F-L26 demonstrated to be a good lead candidates for the labeling of heat sensitive biomolecules with .sup.18F-fluorine and derivatives have been synthesized. We have explored the complexation of {AI.sup.18F}.sup.2+ with new chelators and obtained very favourable radiochemical yields (>85%) using a labeling temperature of 37° C. The stability of the new Al.sup.18F-complexes was tested in phosphate buffered saline (PBS) at pH 7 and in rat serum at 37° C., where AI.sup.18F-L3 and AI.sup.18F-L26 showed a stability comparable to that of the previously reported Al.sup.18F-NODA. Moreover, the biodistribution of Al.sup.18F-L3 and Al.sup.18F-L26 showed high stability, since only very limited bone uptake—which would be an indication of release of fluorine-18 in the form of fluoride—was observed, whereas the major fraction of activity 60 min p.i. was observed in liver and intestines due to hepatobiliary clearance of the radiolabeled ligand. The chelators H.sub.3L3 and H.sub.3L26 demonstrated to be good lead candidates for the labeling of heat sensitive biomolecules with .sup.18F-fluorine and several derivatives have been synthesized.

Provided herein are compositions, kits, and methods for performing analyte detection immunoassays.

Immunoglobulin light chain proteins are used to generate synthetic fibrils in vitro. The fibrils are mixed with immunoglobulin light chain proteins from a biological sample. In either a direct binding assay, competition assay, or dilution-based competition assay, a signal is detected from the mixture. The intensity of the detectable signal relates to the level of binding between the immunoglobulin light chain proteins to the fibrils and can thus be used to identify amyloidogenic immunoglobulin light chain proteins in a biological sample of the subject and to assess amyloidogenic risk to a subject. For example, the signal intensities from the assays can be used in a comparison to one or more threshold (control) values derived from samples of known light chain types or in the absence of light chains. The comparisons permit identification of amyloidogenic proteins, assessment of amyloidogenic risk, and categorization of the subject into an appropriate “at risk” group.

Immunoglobulin light chain proteins are used to generate synthetic fibrils in vitro. The fibrils are mixed with immunoglobulin light chain proteins from a biological sample. In either a direct binding assay, competition assay, or dilution-based competition assay, a signal is detected from the mixture. The intensity of the detectable signal relates to the level of binding between the immunoglobulin light chain proteins to the fibrils and can thus be used to identify amyloidogenic immunoglobulin light chain proteins in a biological sample of the subject and to assess amyloidogenic risk to a subject. For example, the signal intensities from the assays can be used in a comparison to one or more threshold (control) values derived from samples of known light chain types or in the absence of light chains. The comparisons permit identification of amyloidogenic proteins, assessment of amyloidogenic risk, and categorization of the subject into an appropriate “at risk” group.