Amyloid β(1-42) oligomers, derivatives thereof and...

Details Amyloid β(1-42) oligomers, derivatives thereof and... Amyloid β(1-42) oligomers, derivatives thereof and...

2011-03-08

2011-03-08

Chernyshev, Olga N (Department: 1649)

Chemistry: natural resins or derivatives; peptides or proteins;

Peptides of 3 to 100 amino acid residues

25 or more amino acid residues in defined sequence

C530S333000, C530S387100, C514S012200, C424S130100, C424S184100, C424S185100

Reexamination Certificate

active

07902328

ABSTRACT:
The invention relates to neuromodulatory oligomers of the amyloid-β(1-42) protein, a particular production method, by means of which the oligomer can be obtained in a reproducible manner at high yield, the use of the oligomers as diagnostic and therapeutics agents, for the generation of oligomer-specific antibodies and for the discovery of substances which can interact with the oligomers and in the formation thereof. Corresponding methods for the production of the antibodies and for discovery of the substances are also disclosed as are the antibodies themselves and the use of the antibodies or substances as diagnostic and therapeutic agents. The invention further relates to derivatives of the oligomers and oligomers based on abbreviated forms of the amyloid-β(1-42) proteins, the production and use thereof.

REFERENCES:
patent: 6218506 (2001-04-01), Krafft et al.
patent: WO 99/27944 (1999-06-01), None
patent: WO 01/10900 (2001-02-01), None
patent: WO 03/016466 (2003-02-01), None
patent: WO 03/016467 (2003-02-01), None
Kuo et al., J. Biol. Chem.., 1996, vol. 271, No. 8, pp. 4077-4081.
Dahlgren, Karie N. et al. “Oligomeric and fibrillar species of amyloid-beta peptides differentially affect neuronal viability” Journal of Biological Chemistry, Aug. 30, 2002 vol. 277, No. 35, pp. 32046-32053.
N. Demeester et al. “Comparison of the aggregation properties, secondary structure and apoptotic effects of wild-type, Flemish and Dutch N-terminally truncated amyloid beta peptides” European Journal of Neuroscience, Jun. 11, 2001, vol. 13 No. 11, pp. 2015-2024.
Bitan, Gal et al. “Amyloid beta-protein (Abeta) assembly: Abeta40 and Abeta42 oligomerize through distinct pathways” Proceedings of the national Academy of Sciences of the United States Jan. 7, 2003 vol. 100 No. 1, pp. 330-335.
Wurth, C et al. “Mutations that reduce Aggregation of the Alzheimer's Abeta42 Peptide: an Unbiased Search for the Sequence Determinants of Abeta Amyloidogenesis” Journal of Molecular Biology, London, GB Jun. 2002 vol. 319 No. 5, pp. 1279-1290.
Stine, W. Blaine, Jr. et al. “In vitro characterization of conditions for amyloid-beta peptide oligomerization and fibrillogenesis” Journal of Biological Chemistry Mar. 2003 vol. 278 No. 13, pp. 11612-11622.
Roher, A. A. E. et al. “Oligomerization and fibril assembly of the amyloid-beta protein” Biochimica et Biophysica Acta. Molecular Basis of Disease, Amsterdam, NL Jul. 2000 vol. 1502 No. 1 pp. 31-43.
Wilson, D. M. et al. “Free fatty acids stimulate the polymerization of tau and amyloid beta peptides in vitro evidence for a common effector in pathogenesis in Alzheimer's disease” American Journal of Pathology Jun. 1997 vol. 150 No. 6 pp. 2181-2195.
McLaurin, J. et al. “Review Modulating factors in amyloid-beta fibril formation” Journal of Structural Biology Jun. 2000 vol. 130 No. 2-3 pp. 259-270.
Masters, C. L. et al. “Amyloid plaque core protein in Alzheimer disease and Down syndrome” PNAS Jun. 1985 vol. 82 pp. 4245-4249.
Terry, Robert D. et al. “Physical Basis of Cognitive Alterations in Alzheimer's Disease: Synapse Loss Is the Major Correlate of Cognitive Impairment” American Neurological Association 1991 pp. 572-580.
Dickson, Dennis W. et al. “Correlations of Synaptic and Pathological Markers with Cognition of the Elderly”Neurobiology of Aging 1995 vol. 16, No. 3, pp. 285-304.
Lue, Lih-Fen et al. “Soluble Amyloid β Peptide Concentration as a Predictor of Synaptic Change in Alzheimer's Disease” American Journal of Pathology Sep. 1999 vol. 155, No. 3.
McLean, Catriona A. et al. “Soluble Pool of Aβ Amyloid as a Determinant of Severity of Neurodegeneration in Alzheimer's Disease” American Neurological Association 1999 pp. 860-866.
Arispe, Nelson et al. “Alzheimer disease amyloid β protein forms calcium channels in bilayer membranes: Blockage by tromethamine and aluminum” PNAS Jan. 1993 vol. 90 pp. 567-571.
Lashuel, H. A. et al. “Amyloid pores from pathogenic mutations” Nature Jul. 18, 2002 vol. 418 p. 291.
Lambert, M. P. et al. “Diffusible, nonfibrillar ligands derived from A β1-42are potent central nervous system neurotoxins” PNAS May 1998 vol. 95 pp. 6448-6453.
Shenk D. “Amyloid-β immunotherapy for Alzheimer's disease: the end of the beginning” Nature Oct. 2002 vol. 3 pp. 824-828.
Selkoe, Dennis J. “Clearing the Brain's Amyloid Cobwebs” Neuron Oct. 25, 2001 vol. 32 pp. 177-180.
Lee, Edward B. et al. “Secretion and Intracellular Generation of Truncated Aβ in β-Site Amyloid-β Precursor Protein-cleaving Enzyme Expressing Human Neurons” Journal of Biological Chemistry Feb. 14, 2003 vol. 278 No. 7 pp. 4458-4466.
Naslund, Jan et al. “Relative abundance of Alzheimer A β amyloid peptide variants in Alzheimer disease and normal aging” PNAS Aug. 1994 vol. 91 pp. 8378-8382.
Russo, C. et al. “Presenilin-1 mutations in Alzheimer's disease” Nature Jun. 1, 2000 vol. 405 pp. 531-532.
Saido, Takaomi C. et al. “Dominant and Differential Deposition of Distinct β-Amyloid Peptide Species, A βN3(pE), in Senile Plaques” Neuron Feb. 1995 vol. 14 pp. 457-486.
Sergeant, Nicolas et al. “Truncated beta-amyloid peptide species in pre-clinical Alzheimer's disease as new targets for the vaccination approach” Journal of Neurochemistry 2003 vol. 85 pp. 1581-1591.
Laemmli, U. K. et al. “Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4” Nature Aug. 15, 1970 vol. 227 pp. 680-685.
Pike, Chistian J. et al., Structure— Activity Analyses of B-Amyloid Petides: Contributions of the B25-35 Region to Aggregation and Neurotoxicity, J. Neurochem., vol. 64, No. 1, 1995, pp. 253-265.
Kirkitadze, Marina D. et al., Identification and Characterization of Key Kinetic Intermediates in Amyloid B-protein Fibrillogenesis, J. Mol. Biol. (201) 312, 1103-1119.

Affiliated with

Also associated with

Rating

Amyloid β(1-42) oligomers, derivatives thereof and... 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 β(1-42) oligomers, derivatives thereof and..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Amyloid β(1-42) oligomers, derivatives thereof and... will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-2741401