Effect of curcumin on the amyloid fibrillogenesis of hen egg-white lysozyme

被引：89

作者：

Wang, Steven S-S. ^{[1
]}

Liu, Kuan-Nan ^{[1
]}

Lee, Wen-Hsuan ^{[1
]}

机构：

[1] Natl Taiwan Univ, Dept Chem Engn, Taipei 10617, Taiwan

来源：

BIOPHYSICAL CHEMISTRY | 2009年 / 144卷 / 1-2期

关键词：

Lysozyme; Amyloid fibril; Curcumin; Amyloidosis; Inhibitor; HYDROPHOBIC FLUORESCENT-PROBE; RADICAL SCAVENGING ACTIVITY; BETA FIBRIL FORMATION; ALZHEIMERS-DISEASE; IN-VITRO; PRION PROTEIN; ANTIOXIDANT MECHANISM; FOLDING INTERMEDIATE; ALPHA-SYNUCLEIN; PC12; CELLS;

D O I：

10.1016/j.bpc.2009.06.010

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

At least twenty human proteins can fold abnormally to form pathological deposits that are associated with several degenerative diseases. Despite extensive investigation on amyloid fibrillogenesis, its detailed molecular mechanisms remain unknown. This study is aimed at exploring the inhibitory activity of curcumin against the fibrillation of hen lysozyme. We found that the formation of amyloid fibrils at pH 2.0 in vitro was inhibited by curcumin in a dose-dependent manner. Moreover, quenching analysis confirmed the existence of an interaction between curcumin and lysozyme, and Van't Hoff analysis indicated that the curcumin-lysozyme interaction is predominantly governed by Van Der Waals force or hydrogen bonding. Curcumin was also found to acquire disaggregating ability on preformed lysozyme fibrils. Finally, we observed that curcumin pre-incubated at 25 degrees C for at least 7 days inhibited lysozyme fibrillogenesis better than untreated curcumin and the enhanced inhibition against HEWL fibrillation might be attributed to the presence of dimeric species. (C) 2009 Elsevier B.V. All rights reserved.

引用

页码：78 / 87

页数：10

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