Peptide binding the KLVFF-sequence of amyloid-β

Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai

Reexamination Certificate

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

C514S017400, C514S002600, C530S328000, C530S329000

Reexamination Certificate

active

10721774

ABSTRACT:
The invention relates to compounds of formula (I) or (II), which are of interest especially for inhibition of polymerization of amyloid β peptide, as model substances for synthesis of amyloid β peptide-ligands, as tools for the identification of other organic compounds with similar functional properties and/or as ligands for detection of amyloid deposits using e.g., positron emission tomography (PET). Formula (II) is: R1-A′-Y′-Leu-X′-Z′-B′-R2in which X′ means any group or amino acid imparting to the compound according to formula (I) the ability to bind to the KLVFF-sequence in amyloid β peptide, or two amino acids imparting the same ability, but with the proviso that one is not proline; Y′ means any amino acid; Z′ means any non-acidic amino acid; A′ means a direct bond or an α-amino acid bonded at the carboxyl terminal of the α-carboxy group or a di-, tri-, tetra- or pentapeptide bonded at the carboxyl terminal of the α-carboxy group; B′ means a direct bond or an α-amino acid bonded at the α-nitrogen or a di-, tri, tetra- or pentapeptide bonded at the α-nitrogen of the N-terminal α-amino acid; R1is H or —CO—R3bonded at the α-amino group of A′; R2is H, —OR4or NR5R6, all bonded to the α-carboxyl group of the α-carboxyterminal of B′; R3and R4are straight or branched carbon chain of 1-4 carbon atoms; R5and R6are independently H, alkyl, cycloalyl, aryl or substituted aryl or together are —(CH2)n— where n is 4-5; and R1and R2together can form a hydrocarbon ring or heterocyclic ring; all α-amino acids being either D- or L-isomers.

REFERENCES:
patent: 4116768 (1978-09-01), Isowa et al.
patent: 5002872 (1991-03-01), Gross
patent: 5470951 (1995-11-01), Roberts
patent: 5514548 (1996-05-01), Krebber et al.
patent: 5578451 (1996-11-01), Nishimoto
patent: 5593846 (1997-01-01), Schenk et al.
patent: 5652334 (1997-07-01), Roberts
patent: 5688651 (1997-11-01), Solomon
patent: 5721130 (1998-02-01), Seubert et al.
patent: 5753624 (1998-05-01), McMichael et al.
patent: 5780587 (1998-07-01), Potter
patent: 5817626 (1998-10-01), Findeis et al.
patent: 5837672 (1998-11-01), Schenk et al.
patent: 5851996 (1998-12-01), Kline
patent: 5854204 (1998-12-01), Findeis et al.
patent: 5854215 (1998-12-01), Findeis et al.
patent: 5869093 (1999-02-01), Weiner et al.
patent: 5891991 (1999-04-01), Wasco et al.
patent: 5985242 (1999-11-01), Findeis et al.
patent: 6022859 (2000-02-01), Kiessling et al.
patent: 6114133 (2000-09-01), Seubert et al.
patent: 6261569 (2001-07-01), Comis et al.
patent: 6277826 (2001-08-01), Findeis et al.
patent: 6303567 (2001-10-01), Findeis et al.
patent: 6319498 (2001-11-01), Findeis et al.
patent: 6331440 (2001-12-01), Nordstedt et al.
patent: 6436903 (2002-08-01), Clayberger et al.
patent: 6610658 (2003-08-01), Findeis et al.
patent: 6670399 (2003-12-01), Green et al.
patent: 6689752 (2004-02-01), Findeis et al.
patent: 6710226 (2004-03-01), Schenk
patent: 6743427 (2004-06-01), Schenk
patent: 6750324 (2004-06-01), Schenk et al.
patent: 6761888 (2004-07-01), Schenk et al.
patent: 6787138 (2004-09-01), Schenk
patent: 6787139 (2004-09-01), Schenk
patent: 6787140 (2004-09-01), Schenk
patent: 6787143 (2004-09-01), Schenk
patent: 6787144 (2004-09-01), Schenk
patent: 6787523 (2004-09-01), Schenk
patent: 6787637 (2004-09-01), Schenk
patent: 6808712 (2004-10-01), Schenk
patent: 6818218 (2004-11-01), Schenk
patent: 6831066 (2004-12-01), Findeis et al.
patent: 6866849 (2005-03-01), Schenk
patent: 6866850 (2005-03-01), Schenk
patent: 6875434 (2005-04-01), Schenk
patent: 7060670 (2006-06-01), Chalifour et al.
patent: 2004/0157781 (2004-08-01), Nordstedt et al.
patent: 2005/0090439 (2005-04-01), Chalifour et al.
patent: 2006/0199771 (2006-09-01), Chalifour et al.
patent: 199870091 (1998-07-01), None
patent: 0584452 (1994-03-01), None
patent: 0752886 (1998-01-01), None
patent: 0584452 (2002-07-01), None
patent: WO 94/05311 (1994-03-01), None
patent: WO 94/14836 (1994-07-01), None
patent: WO 94/19692 (1994-09-01), None
patent: WO 95/05393 (1995-02-01), None
patent: WO 95/05849 (1995-03-01), None
patent: WO 95/08999 (1995-04-01), None
patent: WO 95/12815 (1995-05-01), None
patent: WO 95/23166 (1995-08-01), None
patent: WO 95/31966 (1995-11-01), None
patent: WO 96/13583 (1996-05-01), None
patent: WO 96/28471 (1996-09-01), None
patent: WO 96/34887 (1996-11-01), None
patent: WO 96/37621 (1996-11-01), None
patent: WO 96/39834 (1996-12-01), None
patent: WO 97/08320 (1997-03-01), None
patent: WO 97/21728 (1997-06-01), None
patent: WO 97/32017 (1997-09-01), None
patent: WO 98/02462 (1998-01-01), None
patent: WO 98/05350 (1998-02-01), None
patent: WO 98/08868 (1998-03-01), None
patent: WO 98/22120 (1998-05-01), None
patent: WO 99/06587 (1999-02-01), None
patent: WO 99/27944 (1999-06-01), None
patent: WO 99/27949 (1999-06-01), None
patent: WO 99/58564 (1999-11-01), None
patent: WO 99/60021 (1999-11-01), None
patent: WO 99/60024 (1999-11-01), None
patent: WO 00/20027 (2000-04-01), None
patent: WO 00/26238 (2000-05-01), None
patent: WO 00/43039 (2000-07-01), None
patent: WO 00/52048 (2000-09-01), None
patent: WO 00/68263 (2000-11-01), None
patent: WO 00/72880 (2000-12-01), None
patent: WO 01/39796 (2001-06-01), None
Camilleri et al., “β-Cyclodextrin Interacts with the Alzheimer Amyloid β-A4 Peptide,” FEBS Letters 341:256-258, 1994.
Fraser et al., “Effects of Sulfate Ions on Alzheimer β/A4 Peptide Assemblies: Implications for Amyloid Fibril-Proteoglycan Interactions,” J. Neurochem. 59:1531-1540, 1992.
Lorenzo et al., “β-Amyloid Neurotoxicity Requires Fibril Formation and is Inhibited by Congo Red,” Proc. Natl. Acad. Sci. USA 91:12243-12247, 1994.
Wood et al., “Prolines and Amyloidogenicity in Fragments of the Alzheimer's Peptide β/A4,” Biochem. 34:724-730, 1995.
Tjernberg et al., “Arrest of β-Amyloid Fibril Formation by a Pentapeptide Ligand”, J. Biol. Chem., 1996, pp. 8545-8548, vol. 271, No. 15, The American Society for Biochemistry and Molecular Biology, Inc., Baltimore, Maryland, USA.
Findeis et al., “Modified-Peptide Inhibitors of Amyloid β-Peptide Polymerization,” Biochem. 38:6791-6800, 1999.
Tjernberg et al., “Controlling Amyloid β-Peptide Fibril Formation with Protease-Stable Ligands,” J. Biol. Chem. 272:12601-12605, 1997.
Alberts, “Molecular Biology of the Cell,” Garland Publishing, p. 54, 1989.
Bard et al., “Peripherally Administered Antibodies Against Amyloid β-Peptide Enter the Central Nervous System and Reduce Pathology in a Mouse Model of Alzheimer Disease, ”Nature Med.6(8):916-919, 2000.
Benkirane et al., “Antigenicity and Immunogenicity of Modified Synthetic Peotides Containing D-Amino Acid Residues, ”J. Biol. Chem.268(35):26278-26285, 1993.
Chen et al., “Neurodegenerative Alzheimer-Like Pathology in PDAPP 717V->F Transgenic Mice, ”Prog. Brain Res.117:327-334, 1998.
Cribbs et al., “All-D-Enantiomers of β-Amyloid Exhibit Similar Biological Properties to All-L-β-Amyloids, ”J. Biol Chem.272(11):7431-7436, 1997.
DeMattos et al., “Peripheral Anti-AβAntibody Alters CNS and Plasma Aβ Clearance and Decreases Brain Aβ Burden in a Mouse Model of Alzheimer's Disease, ”Proc. Nat. Acad. Sci. U.S.A.98(15):8850-8855, 2001.
Findels et al., “Modified-Peptide Inhibitors of Amyloid β-Peptide Polymerization, ”Biochemistry38(21):6791-6800, 1999.
Flood et al., “Topography of a Binding Site for Small Amnestic Peptides Deduced from Structure-Activity Studies: Relation to Amnestic Effect of Amyloid β Protein, ”Proc. Nat. Acad. Sci. U.S.A.91:380-384, 1994.
Frenkel, “Generation of Auto-Antibodies Towards Alzheimer's Disease Vaccination, ”Vaccine19(17-19):2615-2619, 2001.
Frenkel et al., “Immuniza

LandOfFree

Say what you really think

Search LandOfFree.com for the USA inventors and patents. Rate them and share your experience with other people.

Rating

Peptide binding the KLVFF-sequence of amyloid-β does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Peptide binding the KLVFF-sequence of amyloid-β, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Peptide binding the KLVFF-sequence of amyloid-β will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-3853920

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.