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Fullerene inhibits β-amyloid peptide aggregation

Title
Fullerene inhibits β-amyloid peptide aggregation
Authors
Kim J.E.Lee M.
Ewha Authors
이민영
SCOPUS Author ID
이민영scopus
Issue Date
2003
Journal Title
Biochemical and Biophysical Research Communications
ISSN
0006-291XJCR Link
Citation
vol. 303, no. 2, pp. 576 - 579
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
We report that fullerene inhibits strongly the amyloid peptide aggregation at the early stage. It specifically binds to the central hydrophobic motif, KLVFF, of Aβ peptides. The IC50 value has been measured as 9μM for both Aβ11-25 and Aβ1-40. On the other hand, a control experiment shows melatonin rather specifically binds to the C-terminus region. The IC50 value of fullerene appears to be at least four times larger for Aβ1-40, compared with melatonin, and 15 times larger for Aβ11-25. This work shows that fullerene can be a promising candidate in search of AD therapeutics because it has the very high IC50 value for Aβ aggregation. © 2003 Elsevier Science (USA). All rights reserved.
DOI
10.1016/S0006-291X(03)00393-0
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자연과학대학 > 화학·나노과학전공 > Journal papers
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