Abstract: Compositions and methods of non-invasive diagnosis are provided. The imaging agents include a linking groups and a reactive entity capable of reaction with a reactive functionality to form a covalent bond therewith. The imaging agents may be in the form of a bifunctional anchor molecule. The bifunctional anchor molecules have a functional group capable of activation which, when activated, may form a covalent bond with a reactive functionality on a target protein present in the mammalian vascular system, thereby “anchoring” the molecule to that target protein. The bifunctional anchors are also conjugated, either directly or indirectly, to a diagnostic agent of interest which provides the ability to diagnostically and non-invasively image the mammalian vascular space. Vascular targets include both cellular- and noncellular-associated proteins present in the mammalian vascular system.

Abstract: Modified insulinotropic peptides are disclosed. The modified insulinotropic peptides are capable of forming a peptidase stabilized insulinotropic peptide. The modified insulinotropic peptides are capable of forming covalent bonds with one or more blood components to form a conjugate. The conjugates may be formed in vivo or ex vivo. The modified peptides are administered to treat humans with diabetes and other related diseases.

Abstract: Conjugates are prepared from antinociceptive agents, particularly opioids or opioid analogs, more particularly dynorphins, endorphins, deltorphins, enkephalins or analogs thereof, by combining said antinociceptive agent with a material providing a functionally reactive group capable of reacting with a blood component (preferably a blood cell or protein). Said conjugates permit extension of the therapeutic life of the antinociceptive agent. They may be administered to patients to alleviate pain, produce analgesic effects, or assist in cases of narcotics withdrawal, and may also be used as probes for receptor activity.

Abstract: Conjugates are prepared from antinociceptive agents, particularly opioids or opioid analogs, more particularly dynorphins, endorphins, deltorphins, enkephalins or analogs thereof, by combining said antinociceptive agent with a material providing a functionally reactive group capable of reacting with a blood component (preferably a blood cell or protein). Said conjugates permit extension of the therapeutic life of the antinociceptive agent. They may be administered to patients to alleviate pain, produce analgesic effects, or assist in cases of narcotics withdrawal, and may also be used as probes for receptor activity.

Abstract: The present invention relates to peptides which may be used, for example, in the detection of free and complexed Prostate Specific Antigen and thus in the diagnosis of prostate cancer.

Abstract: Novel compounds comprising chemically reactive intermediates which can react with available reactive functionalities on blood components to form covalent linkages, where the resulting covalently-bound conjugates are found to have thrombin inhibition activity are provided. Specifically, the thrombin inhibitor compounds of the present invention are derivatives of the known thrombin inhibitor argatroban, which can be covalently linked to chemically reactive functionalities on various blood components. The conjugated thrombin inhibitors thereby have extended lifetimes in the bloodstream, as compared to the unconjugated parent drug, and are, therefore, capable of maintaining thrombin inhibitory activity for extended periods of time as compared to the unconjugated parent drug. Also provided herein are methods for inhibiting thrombin activity in vivo comprising administering to the bloodstream of a mammalian host the novel compounds of the present invention.

Abstract: This invention relates to genetically engineered enzymes, their ligand conjugates, their manufacture, and their use in qualitative or quantitative assays. A hybrid enzyme, such as an AP-epitope, has a foreign amino acid moiety (an epitope) inserted near the active site of the starting AP enzyme. The foreign amino acid moiety binds with an analyte, and, as a consequence of this binding, the enzymatic activity of the hybrid enzyme, AP-epitope, is modified. The changes in the enzymatic activity are dependent upon the presence, or the amount, of the analyte. In another embodiment, the hybrid enzyme consists of a cysteine introduced near the active site of an AP to give a hybrid enzyme. The cysteine on the hybrid enzyme serves as a point of conjugation of a ligand, such as theophylline, ferritin, thyroxine, or digoxigenin, to form the hybrid enzyme-ligand conjugate.

Abstract: Hepatitis GB Virus (HGBV) synthetic peptides useful for a variety of diagnostic and therapeutic applications, kits for using the HGBV nucleic acid or amino acid sequences and antibodies which specifically bind to HGBV. Also provided are methods for producing antibodies, polyclonal or monoclonal, from the HGBV peptides.

Abstract: HIV-1 peptides having at least one point mutation between position 593 and 611 of the HIV-1 gp160 amino acid sequence. The point mutation either is at position 604 or 610, or both positions. Immunoassays which utilize these peptides are provided, as well as, diagnostic test kits which contain these peptides.

Abstract: HIV-1 peptides having at least one point mutation between position 593 and 611 of the HIV-1 gp160 amino acid sequence. The point mutation either is at position 604 or 610, or both positions. Immunoassays which utilize these peptides are provided, as well as, diagnostic test kits which contain these peptides.