N-terminal EFRH sequence of Alzheimer's β-amyloid peptide represents the epitope of its anti-aggregating antibodies

Journal of Neuroimmunology

Volumn 88, Issue 1-2, 1998, Pages 85-90

  Frenkel, D ^a   Balass, M ^b   Solomon, B ^a  

^a TEL AVIV UNIVERSITY   (Israel)

^b WEIZMANN INSTITUTE OF SCIENCE   (Israel)

Author keywords

amyloid peptide; Disaggregation; Monoclonal antibody; N terminal; Sequential epitope

Indexed keywords

AMYLOID BETA PROTEIN; EPITOPE; MONOCLONAL ANTIBODY;

ALZHEIMER DISEASE; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; CONSENSUS SEQUENCE; ENZYME LINKED IMMUNOSORBENT ASSAY; FLUORESCENCE; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN LOCALIZATION; SENILE PLAQUE;

AMINO ACID SEQUENCE; AMYLOID BETA-PROTEIN; ANTIBODIES, MONOCLONAL; BACTERIOPHAGES; BINDING SITES, ANTIBODY; EPITOPES; FLUORESCENT DYES; PEPTIDE FRAGMENTS; THIAZOLES;

EID: 0032145617     PISSN: 01655728     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0165-5728(98)00098-8     Document Type: Article

References (14)

1. Ashall, F., Goate, A.M., 1994. Role of the β-amyloid precursor protein in Alzheimer disease. TIBS 19, 42-46.
2. Balass, M., Heldman, Y., Cabilly, S., Givol, D., Katchalski-Katzir, E., Fuchs, S., 1993. Identification of a hexapeptide that mimics a conformation-dependent binding site of acetylcholine receptor by use of a phage-epitope library. Proc. Natl. Acad. Sci. U.S.A. 90, 10638-10642.
3. Barrow, C.J., Akikazu, Y., Kenny, P.T.M., Zagorski, M.G., 1992. Solution conformations and aggregational properties of synthetic amyloid β-peptides of Alzheimer's disease. J. Mol. Biol. 225, 1075-1093.
4. Hanan-Aharon, E., Solomon, B., 1996. Inhibitory effect of monoclonal antibodies on Alzheimer's β-amyloid peptide aggregation. Amyloid: Int. J. Exp. Clin. Invest. 3, 130-133.
5. Hilbich, C., Kisters-Waike, B., Masters, C.L., Beyreuther, K., 1994. Amyloid β-A4 of Alzheimer's disease: structural requirements for folding and aggregation. In: Masters, C.L., et al. (Eds.), Amyloid Protein Precursor in Development Aging and Alzheimer's Disease. Springer-Verlag, Berlin.
6. Levine, H. III, 1993. Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci. 2, 404-410.
7. Maggio, J.E., Stimson, E.R., Ghilardi, J.R., Allen, C.J., Dahl, C.E., Whitcomb, D.C., Vigna, S.R., Vinters, H.V., Labenski, M.E., Mantyh, P.W., 1992. Reversible in vitro growth of Alzheimer disease β-amyloid plaques by deposition of labeled amyloid peptide. Proc. Natl. Acad. Sci. U.S.A. 89, 5462-5466.
8. Medynski, D., 1994. Phage display: all dressed up and ready to role. Biol. Technol. 12, 1134-1136.
9. Pinkard, R.N., Weir, D.M., 1978. In: Weir, D.M. (Ed.), Handbook of Experimental Immunology. Blackwell, Oxford, pp. 16.1-16.20.
10. Scott, J.K., 1992. Discovering peptide ligands using epitope libraries. TIBS 241-245.
11. Scott, J.K., Smith, G.P., 1990. Searching for peptide ligands with an epitope library. Science 249, 386-390.
12. Selkoe, D.J., 1991. The molecular pathology of Alzheimer disease. Neuron 6, 487-498.
13. Solomon, B., Koppel, R., Frenkel, D., Hanan-Aharon, E., 1997. Disaggregation of Alzheimer β-amyloid by site-directed mAb. Proc. Natl. Acad. Sci. U.S.A. 94, 4109-4112.
14. Soto, C., Kindy, M.S., Baumann, M., Frangione, B., 1996. Inhibition of Alzheimer's amyloidosis by peptides that prevent β-sheet conformation. Biochem. Biophys. Res. Commun. 226 (3), 672-680.