Practical assay and molecular mechanism of aggregation inhibitors of β-amyloid

Journal of Peptide Research

Volumn 61, Issue 1, 2003, Pages 1-6

  Akikusa, S ^a,b   Nakamura, Kazuhiko ^a   Watanabe, K I ^a,b   Horikawa, E ^a,b   Konakahara, T ^b   Kodaka, M ^a   Okuno, H ^a  

^a NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

^b TOKYO UNIVERSITY OF SCIENCE   (Japan)

Author keywords

amyloid; Aggregation inhibitor; Alzheimer's disease; Fluorescence assay; Molecular interaction; Multipin

Indexed keywords

AMYLOID BETA PROTEIN;

ALZHEIMER DISEASE; ARTICLE; FLUORESCENCE ANALYSIS; MOLECULAR INTERACTION; NEUROTOXICITY; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN STRUCTURE; SENILE PLAQUE;

AMINO ACID SEQUENCE; AMYLOID BETA-PROTEIN; BINDING, COMPETITIVE; FLUORESCENT DYES; HUMANS; HYDROPHOBICITY; MODELS, CHEMICAL; MOLECULAR SEQUENCE DATA; OLIGOPEPTIDES; PROTEIN BINDING; SPECTROMETRY, FLUORESCENCE;

EID: 0037229254     PISSN: 1397002X     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1399-3011.2003.21028.x     Document Type: Article

References (17)

1. Sipe, J.D. & Cohen, A.S. (2000) History of amyloid fibril. J. Struct. Biol. 130, 88-98.
2. Esler, W.P., Stimson, E.R., Mantyh, P.W. & Maggio, J.H. (1999) Deposition of soluble amyloid-β onto amyloid templates: identification of amyloid fibril extension inhibitors. In: Methods in Enzymotogy 309 (Wetzel, R., ed.). Academic Press, London, pp. 350-374.
3. Selkoe, D.J. (1999) Translating cell biology into therapeutic advances in Alzheimer's disease. Nature 399, A23-A31.
4. Simmons, L.K., May, P.C., Tomaselli, K.J., Rydel, R.E., Fuson, K.S., Brigham, E.F., Wright, S., Lieberburg, I., Becker, G.W., Brems, D.N. & Li, W.Y. (1994) Secondary structure of amyloid beta peptide correlates with neurotoxic activity in vitro. Mol. Pharmacol. 45, 373-379.
5. Serpell, L.C. (2000) Alzheimer's amyloid fibrils: structure and assembly. Biochim. Biophys. Acta 1502, 16-30.
6. Findeis, M.A., Musso, G.M., Arico-Muendel, C.C., Benjamin, H.W., Hundal, A.M., Lee, J.-J., Chin, J., Kelley, M., Wakefield, J., Hayward, N.J. & Molineaux, S.M. (1999) Modified-peptide inhibitors of amyloid β-peptide polymerization. Biochemistry 38, 6791-6800.
7. Pallitto, M.M., Ghanta, J., Heinzelman, P., Kiessling, L.L. & Murphy, R.M. (1999) Recognition sequence design for peptidyl modulators of β-amyloid aggregation and toxicity. Biochemistry 38, 3570-3578.
8. Lowe, T.L., Strzelec, A., Kiessling, L.L. & Murphy, R.M. (2001) Structure-function relationships for inhibitors of β-amyloid toxicity containing the recognition sequence KLVFF. Biochemistry 40, 7882-7889.
9. Gordon, D.J., Sciarretta, K.L. & Meredith, S.C. (2001) Inhibition of β-Amyloid(40) fibrillogenesis and disassembly of β-amyloid(40) fibrils by short β-amyloid congeners containing N-methyl amino acids at alternate residues. Biochemistry 40, 8237-8245.
10. Soto, C., Sigurdsson, E.M., Morelli, L., Kumar, A., Castaño, E.M. & Frangion, B. (1998) Beta-sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: implications for Alzheimer's therapy. Nature Med. 4, 822-826.
11. Tjernberg, L.O., Näslund, J., Lindqvist, F., Johansson, J., Karlsröm, A.R., Thyberg, J., Terenius, L. & Nordstedt, C. (1996) Arrest of beta-amyloid fibril formation by a pentapeptide ligand. J Biol. Chem. 271, 8545-8548.
12. Tjernberg, L.O., Lilliehöök, C., Callaway, D.J.E., Näslund, J., Hahne, S., Thyberg, J., Terenius, L. & Nordstedt, C. (1997) Controlling amyloid beta-peptide fibril formation with protease-stable ligands. J. Biol. Chem. 272, 12601-12605.
13. Watanabe, K., Nakamura, K., Akikusa, S., Okada, T., Kodaka, M., Konakahara, T. & Okuno, H. (2002) Inhibitors of fibril formation and cytotoxicity of β-amyloid peptide composed of KLVFF recognition element and flexible hydrophilic disrupting element. Biochem. Biophys. Res. Commun. 290, 121-124.
14. Watanabe, K., Segawa, T., Nakamura, K., Kodaka, M., Konakahara, T. & Okuno, H. (2001) Identification of the molecular interaction site of amyloid β peptide by using a fluorescence assay. J. Peptide Res. 58, 342-346.
15. 1H NMR of Aβ amyioid peptide congeners in water solution. Conformational changes correlate with plaque competence. Biochemistry 34, 5191-5200.
16. Esler, W.P., Stimson, E.R., Ghilardi, J.R., Lu, Y.A., Felix, A.M., Vinters, H.V., Mantyh, P.W., Lee, J.P. & Maggio, J.E. (1996) Point substitution in the central hydrophobic cluster of a human β-amyloid congener disrupts peptide folding and abolishes plaque competence. Biochemistry 35, 13914-13921.
17. Conway, K.A., Lee, S.-J., Rochet, J.-C., Ding, T.T., Williamson, R.E. & Lansbury, P.T. (2000) Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy. Proc. Natl Acad. USA 97, 571-576.