The Polyphenol EGCG Inhibits Amyloid Formation Less Efficiently at Phospholipid Interfaces than in Bulk Solution

被引:115
作者
Engel, Maarten F. M. [1 ]
VandenAkker, Corianne C. [1 ]
Schleeger, Michael [1 ,2 ]
Velikov, Krassimir P. [3 ,4 ]
Koenderink, Gijsje H. [1 ]
Bonn, Mischa [1 ,2 ]
机构
[1] FOM Inst AMOLF, NL-1098 XG Amsterdam, Netherlands
[2] Max Planck Inst Polymer Res, Dept Mol Spect, D-55128 Mainz, Germany
[3] Unilever Res Labs, NL-3133 AT Vlaardingen, Netherlands
[4] Univ Utrecht, Debye Inst Nanomat Sci, Dept Phys & Astron, NL-3584 CC Utrecht, Netherlands
关键词
SUM-FREQUENCY GENERATION; MEROZOITE SURFACE PROTEIN-2; BETA-SHEET STRUCTURES; FIBRIL FORMATION; IN-SITU; MEMBRANE INTERACTION; MISFOLDING DISEASES; ALPHA-SYNUCLEIN; LIPID-BILAYERS; POLYPEPTIDE;
D O I
10.1021/ja3031664
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Age-related diseases, like Alzheimer's disease and type 2 diabetes mellitus, are characterized by protein misfolding and the subsequent pathological deposition of fibrillized protein, also called amyloid. Several classes of amyloid-inhibitors have recently been tested, traditionally under bulk conditions. However, it has become apparent that amyloid fibrils and oligomers assemble and exert their cytotoxic effect at cellular membranes, rather than in bulk solution. Knowledge is therefore required of inhibitor activity specifically at the phospholipid membrane interface. Here we show, using surface-specific sum-frequency generation (SFG) spectroscopy and atomic force microscopy (AFM), that the commonly used (-)-epigallocatechin gallate (EGCG) is a much less efficient amyloid inhibitor at a phospholipid interface than in bulk solution. Moreover, EGCG is not able to disaggregate existing amyloid fibrils at a phospholipid interface, in contrast to its behavior in bulk. Our results show that interfaces significantly affect the efficiency of inhibition by EGCG inhibitors and should therefore be considered during the design and testing of amyloid inhibitors.
引用
收藏
页码:14781 / 14788
页数:8
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