Organic compounds -- part of the class 532-570 series – Organic compounds – Heavy metal containing
Reexamination Certificate
2007-07-31
2007-07-31
Kumar, Shailendra (Department: 1621)
Organic compounds -- part of the class 532-570 series
Organic compounds
Heavy metal containing
C564S305000, C564S441000, C564S443000, C558S418000, C558S411000, C514S525000, C514S646000, C514S739000, C424S001110, C424S001650, C424S001810, C424S001850, C424S001890
Reexamination Certificate
active
10228275
ABSTRACT:
This invention relates to a method of imaging amyloid deposits and to labeled compounds, and methods of making labeled compounds useful in imaging amyloid deposits. This invention also relates to compounds, and methods of making compounds for inhibiting the aggregation of amyloid proteins to form amyloid deposits, and a method of delivering a therapeutic agent to amyloid deposits.
REFERENCES:
patent: 5525632 (1996-06-01), Obsumi et al.
patent: 5601801 (1997-02-01), Flanagan et al.
Journal of Organometallic Chemistry, 96(1975)237-241.
Journal of Medicinal Chemistry, (1978), 21(9), 889-91.
Journal of The Chemical Society, Perkin Transaction 2 Physical Organic Chemistry, (1972-1993), (1977), (8), 1051-7.
Marina et al., Journal of Labelled Compounds and Radiopharmaceuticals, vol. XX, No. 4, 501-514, 1983.
Ashburn, T.T.,et al., “Amyloid probes based on Congo Red distinguish between fibrils comprising different peptides,”Chem. Biol., 3:351-358, Current Biology, Ltd. (1996).
Berge, S.M.,et al., “Pharmaceutical Salts,”J. Pharm. Sci.66:1-19, American Pharmaceutical Association (1977).
Elhaddaoui, A.,et al., “Competition of Congo Red and Thioflavin S Binding to Amyloid Sites in Alzheimer's Diseased Tissue,”Biospectroscopy 1:351-356, John Wiley & Sons, Ltd. (1995).
Findeis, M.A., “Approaches to discovery and characterization of inhibitors of amyloid β-peptide polymerization,”Biochim. Biophys. Acta1502:76-84, Elsevier Science B.V. (Jul. 2000).
Ginsberg, S.D., et al., “Molecular Pathology of Alzheimer's Disease and Related Disorders,” inCereb. Cortex, Peters, A., and Morrison, J.H., eds., Kluwer Academic/Plenum Publishers, New York, NY, pp. 603-654 (1999).
Golde, T.E., et al., “Biochemical detection of Aβisoforms: implications for pathogenesis, diagnosis, and treatment of Alzheimer's disease,”Biochim. Biophys. Acta1502:172-187, Elsevier Science B.V. (Jul. 2000).
Han, H., et al., “Technetium Complexes for the Quantitation of Brain Amyloid,”J. Am. Chem. Soc. 118:4506-4507, American Chemical Society (1996).
Klunk, W.E., et al., “Quantitative Evaluation of Congo Red Binding to Amyloid-like Proteins with a Beta-pleated Sheet Conformation,”J. Histochem. Cytochem. 37:1273-1281, Histochemical Society, Inc. (1989).
Klunk, W.E., et al., “Quantitative in vitro NMR analysis of Alzheimer's, non-Alzheimer's demented and control brain,”Biol. Psychiatry(Abstracts)35-627, Abstract No. 44., Elsevier (1994).
Klunk, W.E., et al., “Chrysamine-G Binding to Alzheimer and Control Brain: Autopsy Study of a New Amyloid Probe,”Neurobiol. Aging 16:541-548, Elsevier Science, Ltd. (1995).
Klunk, W.E., et al., “Staining of AD and Tg2576 mouse brain with X-34, a highly fluorescent derivative of chrysamine G and a potential in vivo probe for β-sheet fibrils,”Abstr. Soc. Neurosci. 23:1638, Abstract No. 636.12, Society for Neuroscience (1997).
Kuner, P., et al., “Controlling Polymerization of β-Amyloid and Prion-derived Peptides with Synthetic Small Molecule Ligands,”J. Biol. Chem. 275:1673-1678, American Society for Biochemistry and Molecular Biology, Inc. (Jan. 2000).
Lorenzo, A., and Yankner, B.A., “β-Amyloid neurotoxicity requires fibril formation and is inhibited by Congo red,”Proc. Natl. Acad. Sci. USA91:12243-12247, National Academy Press (1994).
Mathis, C.A., et al., “Synthesis of a lipophilic, radioiodinated ligand with high affinity to amyloid protein in Alzheimer's disease brain tissue,”J. Labelled Cpd. Radiopharm. 40:94-95, John Wiley & Sons, Ltd. (1997).
Moore, C.L., et al., “Difluoro Ketone Peptidomimetics Suggest a Large S1 Pocket for Alzheimer's γ-Secretase: Implications for Inhibitor Design,”J. Med. Chem. 43:3434-3442, American Chemical Society (Sep. 2000).
Näslund, J., et al., “Correlation Between Elevated Levels of Amyloid β-Peptide in the Brain and Cognitive Decline,”JAMA 283:1571-1577, American Medical Association (Mar. 2000).
Selkoe, D.J., “Biology of β-Amyloid Precursor and the Mechanism of Alzheimer Disease,” inAlzheimer Disease, 2ndedition, Terry, R.D., et al., eds., Lippincott Williams & Wilkens, Philadelphia, PA, pp. 293-310 (1999).
Selkoe, D.J., “The Origins of Alzheimer Disease. A is for Amyloid,”JAMA 283:1615-1617, American Medical Association (Mar. 2000).
Skovronsky, D.M., and Lee, V. M.-Y., “β-Secretase revealed: starting gate for race to novel therapies for Alzheimer's disease,”Trends Pharmacol. Sci. 21:161-163, Elsevier (May 2000).
Vassar, R., et al., “β-Secretase Cleavage of Alzheimer's Amyloid Precursor Protein by the Transmembrane Aspartic Protease BACE,”Science 286:735-741, American Association for the Advancement of Science (1999).
Vogelsberg-Ragaglia, V., et al., “Cell Biology of Tau and Cytoskeletal Pathology in Alzheimer Disease,” inAlzheimer Disease, 2ndedition, Terry, R.D., et al., eds., Lippincott Williams & Wilkins, Philadelphia, PA, pp. 359-372 (1999).
Wolfe, M.S., et al., “A Substrate-Based Difluoro Ketone Selectively Inhibits Alzheimer's γ-Secretase Activity,”J. Med. Chem. 41:6-9, American Chemical Society (1998).
Xia, W., et al., “Presenilin complexes with the C-terminal fragments of amyloid precursor protein at the sites of amyloid β-protein generation,”Proc. Natl. Acad. Sci. USA 97:9299-9304, National Academy Press (Aug. 2000).
Zhen, W., et al., “Synthesis and Amyloid Binding Properties of Rhenium Complexes: Preliminary Progress Toward a Reagent for SPECT Imaging of Alzheimer's Disease Brain,”J. Med. Chem. 42:2805-2815, American Chemical Society (1999).
Arbez-Gindre, C., et al., “Organolithium reagents bearing nonlinear optical chromophores. Synthesis of triarylmethane dyes,”Tetrahedron Lett. 40:7413-7416, Elsevier Science, Ltd. (1999).
Lee, C-W., et al., “Isomerization of (Z,Z) to (E,E) 1-Bromo-2,5-bis-(3-hydroxycarbonyl-4-hydroxyl)-styrylbenzene in Strong Base: Probes for Amyloid Plaques in the Brain,”J. Med. Chem. 44:2270-2275, American Chemical Society (Jul. 2001).
Zhuang, Z.-P., et al., “Radioiodinated Styrylbenzenes and Thioflavins as Probes for Amyloid Aggregates,”J. Med. Chem. 44:1905-1914, American Chemical Society (Jun. 2001).
Database CAPLUS on STN, Chemical abstracts, Accession No. 1976:73777, Tewari et al., “Generation and reactions of some dimethyl benzylphosphonate carbanions: synthesis of trans-diaryl-substituted ethylenes,”J. Chem. Eng. Data 21(1):125-131 (1976), abstract.
International Search Report for International Application No. PCT/US02/27201 mailed on Dec. 20, 2002.
Counsell, R.E., et al., “Radioiodinated Estrogens and Antiestrogens as Potential Imaging Agents,” Current Topics in Molecular Endocrinology, 4)Steroid Horm. Action Cancer, pp. 107-113, Lab. of Med. Chem. Coll. of Pharm. Univ. of Mich., Ann Arbor (1976).
Krujier, P.S., et al., “Biodistribution of123I-Labeled 4-Hydroxytamoxifen Derivatives in Rats with Dimethylbenzanthracene-Induced Mammary Carcinomas,”Nucl. Med. & Biol.24:719-722 (1997).
Kung, H.F., et al., “Novel Stilbenes as Probes for Amyloid Plaques,”J. Am. Chem. Soc.,123:12740-12741, American Chemical Society (2001).
Supplementary Partial European Search Report for European Patent Application No. EP 02757398.9, European Patent Office, mailed Aug. 24, 2006.
Ho, T.-I., et al., “Novel Photochemical Rearrangement of Styrylfurans,”Angew. Chem. Int. Ed. Engl.38:2558-2560, Verlag Chemie (1999).
Holand, S., et al., “Acetylenic glycols. VI. Relation between the structure and the cyclization ability in alkaline medium,”Chemical Abstracts 78,American Chemical Society, Abstract No. 71798 (1973).
Supplementary Partial European Search Report for European Patent Application No. EP 02757398.9, E
Kung Hank F.
Kung Mei-Ping
Zhuang Zhi-Ping
Kumar Shailendra
Sterne Kessler Goldstein & Fox PLLC
The Trustees of the University of Pennsylvania
LandOfFree
Stilbene derivatives and their use for binding and imaging... does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Stilbene derivatives and their use for binding and imaging..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Stilbene derivatives and their use for binding and imaging... will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-3807563