(-)-Epicatechin gallate prevents alkali-salt mediated fibrillogenesis of hen egg white lysozyme

被引:56
作者
Ghosh, Sudeshna [1 ]
Pandey, Nitin K. [1 ]
Dasgupta, Swagata [1 ]
机构
[1] Indian Inst Technol, Dept Chem, Kharagpur 721302, W Bengal, India
关键词
Fibrillation; Hen egg white lysozyme; (-)-Epicatechin gallate (ECG); Inhibition; AMYLOID FIBRIL FORMATION; MEROZOITE SURFACE PROTEIN-2; HUMAN SERUM-ALBUMIN; GREEN TEA; (-)-EPIGALLOCATECHIN GALLATE; ALZHEIMERS-DISEASE; CIRCULAR-DICHROISM; TERTIARY BUTANOL; BETA OLIGOMERS; IN-VIVO;
D O I
10.1016/j.ijbiomac.2012.11.031
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
Green tea polyphenols (GTPs) are found to be potent inhibitors of amyloid fibril formation. We report the effective inhibitory property of (-)-epicatechin gallate (ECG) during the alkali-salt induced fibrillogenesis of hen egg white lysozyme (HEWL) at 37 degrees C. Spectroscopic techniques such as fluorescence, circular dichroism and microscopic images show that (-)-epigallocatechin (EGC), (-)-epicatechin gallate (ECG), and (-)-epigallocatechin gallate (EGCG) show moderate inhibition of fibrillation with ECG as the most potent polyphenol. Aromatic interactions, hydrophobic interactions, the radical scavenging activity and autoxidation of polyphenols are likely to be the major reasons for ECG being the most effective inhibitor. (c) 2012 Elsevier B.V. All rights reserved.
引用
收藏
页码:90 / 98
页数:9
相关论文
共 62 条
[1]   Identification and Characterization of Molten Globule-Like State of Hen Egg-White Lysozyme in Presence of Salts Under Alkaline Conditions [J].
Ansari, M. A. ;
Zubair, S. ;
Atif, S. M. ;
Kashif, M. ;
Khan, N. ;
Rehan, M. ;
Anwar, T. ;
Iqbal, A. ;
Owais, M. .
PROTEIN AND PEPTIDE LETTERS, 2010, 17 (01) :11-17
[2]   Anti-amyloidogenic and fibril-destabilizing effects of two manganese-salen derivatives against hen egg-white lysozyme aggregation [J].
Bahramikia, Seifollah ;
Yazdanparast, Razieh .
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, 2012, 50 (01) :187-197
[3]   Molecular Mechanism of Thioflavin-T Binding to the Surface of β-Rich Peptide Self-Assemblies [J].
Biancalana, Matthew ;
Makabe, Koki ;
Koide, Akiko ;
Koide, Shohei .
JOURNAL OF MOLECULAR BIOLOGY, 2009, 385 (04) :1052-1063
[4]   EGCG remodels mature α-synuclein and amyloid-β fibrils and reduces cellular toxicity [J].
Bieschke, Jan ;
Russ, Jenny ;
Friedrich, Ralf P. ;
Ehrnhoefer, Dagmar E. ;
Wobst, Heike ;
Neugebauer, Katja ;
Wanker, Erich E. .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2010, 107 (17) :7710-7715
[5]   STRUCTURE OF HEN EGG-WHITE LYSOZYME - A 3-DIMENSIONAL FOURIER SYNTHESIS AT 2A RESOLUTION [J].
BLAKE, CCF ;
KOENIG, DF ;
MAIR, GA ;
NORTH, ACT ;
PHILLIPS, DC ;
SARMA, VR .
NATURE, 1965, 206 (4986) :757-&
[6]   EGCG disaggregates amyloid-like fibrils formed by Plasmodium falciparum merozoite surface protein 2 [J].
Chandrashekaran, Indu R. ;
Adda, Christopher G. ;
MacRaild, Christopher A. ;
Anders, Robin F. ;
Norton, Raymond S. .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 2011, 513 (02) :153-157
[7]   Inhibition by Flavonoids of Amyloid-like Fibril Formation by Plasmodium falciparum Merozoite Surface Protein 2 [J].
Chandrashekaran, Indu R. ;
Adda, Christopher G. ;
MacRaild, Christopher A. ;
Anders, Robin F. ;
Norton, Raymond S. .
BIOCHEMISTRY, 2010, 49 (28) :5899-5908
[8]   Oxidative stress and Alzheimer disease [J].
Christen, Y .
AMERICAN JOURNAL OF CLINICAL NUTRITION, 2000, 71 (02) :621S-629S
[9]   Targeting the neurotoxic species in Alzheimer's disease:: inhibitors of Aβ oligomerization [J].
De Felice, FG ;
Vieira, MNN ;
Saraiva, LM ;
Figueroa-Villar, JD ;
Garcia-Abreu, J ;
Liu, R ;
Chang, L ;
Klein, WL ;
Ferreira, ST .
FASEB JOURNAL, 2004, 18 (12) :1366-1372
[10]   Inhibition of Alzheimer's disease β-amyloid aggregation, neurotoxicity, and in vivo deposition by nitrophenols:: implications for Alzheimer's therapy [J].
De Felice, FG ;
Houzel, JC ;
Garcia-Abreu, J ;
Louzada, PRF ;
Afonso, RC ;
Meirelles, MNL ;
Lent, R ;
Neto, VM ;
Ferreira, ST .
FASEB JOURNAL, 2001, 15 (07) :1297-1299