Drug – bio-affecting and body treating compositions – Radionuclide or intended radionuclide containing; adjuvant... – In an organic compound
Reexamination Certificate
2005-09-20
2005-09-20
Jones, Dameron L. (Department: 1616)
Drug, bio-affecting and body treating compositions
Radionuclide or intended radionuclide containing; adjuvant...
In an organic compound
C424S001110, C424S001650, C424S001810, C424S001850, C544S235000, C548S300100
Reexamination Certificate
active
06946116
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: 5869500 (1999-02-01), Trottmann et al.
patent: 6037473 (2000-03-01), Dilk et al.
patent: 6168776 (2001-01-01), Klunk et al.
patent: 6696039 (2004-02-01), Kung et al.
patent: 0 659 418 (1995-06-01), None
patent: WO 95/06469 (1995-03-01), None
patent: WO 97/41856 (1997-11-01), None
patent: WO 98/17267 (1998-04-01), None
patent: WO 99/24394 (1999-05-01), None
patent: WO 02/085903 (2002-10-01), None
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).
Bottin-Strzalko, T., and Seyden-Penne, J., “La réaction de Wittig-Horner á partir de phosphonate benzylique permet-elle la synthése de stilbéne cis ?”Bull. Soc. Chim. Fr.(3-4, Pt. 2):161-163, Bayeaux Société Francaise De Chimie (1984).
Bottin-Strzalko, T., and Seyden-Penne, J., “Could cis-stilbene be prepared from benzylic phosphonate by a Wittig-Horner reaction?” CAplus, Accession No. 1984:570794 (1984).
Dezutter, N.A., et al., “Preparation and biological evaluation of technetium-99m-L,L-propylenedicysteine,”J. Labelled Cpd. Radiopharm.42:553-565, John Wiley & Sons, Ltd. (1999).
Dezutter, N.A., et al., “99mTc-MAMA-chrysamine G, a probe for beta-amyloid protein of Alzheimer's disease,”Eur. J. Nucl. Med. 26:1392-1399, Springer-Verlag (1999).
Elhaddaoui, A., et al., “Competition of Congo Red and Thioflavin S Binding to Amyloid Sites in Alzheimer's Diseased Tissue,”Biospectroscopy1:351-356, John Wiley & Sons, Ltd. (1995).
Filler, R. et al., “Synthesis of fluorovinylsalicylic acids and their derivatives,”J. Fluor. Chem. 74:69-75, Elsevier (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 Aβ isoforms: implicaitions for pathogenesis, diagnois, 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).
Katz, T.J., et al., “Synthesis and Properties of Optically Active Helical Metallocene Oligomers,”J. Am. Chem. Soc. 115:3182-3198, American Chemical Society (1993).
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. Aging16:541-548, 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 Molecular Ligands,”J. Biol. Chem.275:1673-1678, American Society for Biochemistry and Molecular Biology, Inc. (Jan. 2000).
Kung, M.-P., et al., “Characterization of [123l]IDAM as a novel single-photon emission tomography tracer for serotonin transporters,”Eur. J. Nucl. Med. 26:844-853, Springer-Verlag (1999).
Kurihara, A., and Pardridge, W.M., “Aβ1-40Peptide Radiopharmaceuticals for Brain Amyloid Imaging:111In Chelation, Conjugation to Poly(ethylene glycol)-Biotin Linkers, and Autoradiography with Alzheimer's Disease Brain Sections,”Bioconjug. Chem. 11:380-386, American Chemical Society (May/Jun. 2000).
Lin, A.J., and Kasina, S., “Synthesis of 3-Substituted 7-(3,3-Dimethyl-1-triazeno)-10-methylphenothiazines as Potential Antitumor Agents,”J. Heterocycl. Chem. 18:759-761, HeteroCorporation (1981).
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).
Mital, R.L., and Jain, S.K., “Synthesis of Some 5-Substituted 2-Aminobenzenethiols and their Conversion into Phenothiazines via Smiles Rearrangement,”J. Chem. Soc. (C) 16:2148-2150, Royal Society of Chemistry (1969).
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,”JAMA283:1571-1577, American Medical Association (Mar. 2000).
Selkoe, D.J., “Biology of β-Amyloid Precursor Protein and the Mechanism of Alzheimer Disease,” inAlzheimer Disease, 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,”JAMA283:1615-1617, American Medical Association (Mar. 2000).
Selkoe, D.J., “Imaging Alzheimer's amyloid,”Nat. Biotechnol. 18:823-824, Nature Publishing Company (Aug. 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).
Skovronsky, D.M., et al., “In vivo detection of amyloid plaques in a mouse model of Alzheimer's disease,”Proc. Natl. Acad. Sci. USA97:7609-7614, National Acadamy Press (Jun. 2000).
Stevens, M.F.G., et al., “Structural Studies on Bioactive Compounds. 23. Synthesis of Polyhydroxylated 2-Phenylbenzothiazoles and a Comparison of Their Cytotoxicites and Pharmacological Properties with Genistein and Quercetin,”J. Med. Chem. 37:1689-1695, American Chemical Society (1994).
Styren, S.D., et al., “X-34, A Fluorescent Derivative of Congo Red: A Novel Histochemical Stain for Alzheimer's Disease Pathology,”J. Histochem. Cytochem. 48:1223-1232, Histochemical Society, Inc. (Sep. 2000).
Tanaka, A., et al., “Inhibitors of Acyl-CoA:Cholesterol O-Acyltransferase. 2. Identification and Structure-Activity Relationships of a Novel Series of N-Alky-N-(heteroaryl-substituted benzyl)-N'-arylurease,”J. Med. Chem. 41:2390-2410, American Chemical Society (1998).
Twyman, L.J., and Allsop, D., “A Short Synthesis of the β-amyloid (Aβ) Aggregation Inhibitor 3-ρ-Toluoyl-2-[4'-(3-diethylaminopr
Kung Hank F.
Kung Mei-Ping
Zhuang Zhi-Ping
Jones Dameron L.
Sterne Kessler Goldstein & Fox P.L.L.C.
The Trustees of the University of Pennsylvania
LandOfFree
Amyloid plaque aggregation inhibitors and diagnostic 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 Amyloid plaque aggregation inhibitors and diagnostic imaging..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Amyloid plaque aggregation inhibitors and diagnostic imaging... will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-3385059