Ferulic acid destabilizes preformed {beta}-amyloid fibrils in vitro

Journal Article · Fri Oct 21 00:00:00 EDT 2005 · Biochemical and Biophysical Research Communications

DOI:https://doi.org/10.1016/j.bbrc.2005.08.148· OSTI ID:20713382

Ono, Kenjiro ^[1]; Hirohata, Mie ^[1]; Yamada, Masahito ^[1]

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1. Department of Neurology and Neurobiology of Aging, Kanazawa University Graduate School of Medical Science, Kanazawa 920-8640 (Japan)

Inhibition of the formation of {beta}-amyloid fibrils (fA{beta}), as well as the destabilization of preformed fA{beta} in the CNS, would be attractive therapeutic targets for the treatment of Alzheimer's disease (AD). We reported previously that curcumin (Cur) inhibits fA{beta} formation from A{beta} and destabilizes preformed fA{beta} in vitro. Using fluorescence spectroscopic analysis with thioflavin T and electron microscopic studies, we examined the effects of ferulic acid (FA) on the formation, extension, and destabilization of fA{beta} at pH 7.5 at 37 deg C in vitro. We next compared the anti-amyloidogenic activities of FA with Cur, rifampicin, and tetracycline. Ferulic acid dose-dependently inhibited fA{beta} formation from amyloid {beta}-peptide, as well as their extension. Moreover, it destabilized preformed fA{beta}s. The overall activity of the molecules examined was in the order of: Cur > FA > rifampicin = tetracycline. FA could be a key molecule for the development of therapeutics for AD.

• OSTI ID: 20713382
• Journal Information: Biochemical and Biophysical Research Communications, Vol. 336, Issue 2; Other Information: DOI: 10.1016/j.bbrc.2005.08.148; PII: S0006-291X(05)01782-1; Copyright (c) 2005 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
• Country of Publication: United States
• Language: English

Related Subjects

60 APPLIED LIFE SCIENCES
CURCUMIN
ELECTRON MICROSCOPY
FLUORESCENCE
IN VITRO
INHIBITION
NERVOUS SYSTEM DISEASES
PEPTIDES
PH VALUE
TETRACYCLINES