Amyloid - Membrane Interactions: Experimental Approaches and Techniques

被引:16
|
作者
Jelinek, Raz [1 ]
Sheynis, Tania [1 ]
机构
[1] Ben Gurion Univ Negev, Dept Chem, IL-84105 Beer Sheva, Israel
关键词
Amyloid; membrane; membrane interactions; amyloidogenic peptides; proteins emanates; ALPHA-SYNUCLEIN; BETA-PROTEIN; CHANNEL FORMATION; PRION PROTEIN; A-BETA; SECONDARY STRUCTURE; HUMAN CALCITONIN; LIPID-BILAYERS; ION CHANNELS; PHOSPHOLIPID-MEMBRANES;
D O I
10.2174/138920310791330640
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
The growing interest in membrane interactions of amyloidogenic peptides and proteins emanates from the realization that lipids and membranes play important, potentially central, roles in the toxicity and pathological pathways of amyloid diseases. Expanding body of evidence indicates that lipid binding of amyloidogenic peptides and amyloid peptide association with cellular membranes is critical in the onset and progression of amyloid diseases. Advancing the understanding in this field goes hand in hand with application of varied biophysical and biological techniques designed to probe the characteristics and underlying mechanisms of membrane-peptide interactions. This review summarizes experimental approaches and technical aspects employed in recent years for investigating the interaction of amyloid peptides and fibrillar species with lipid bilayers, and the reciprocal contribution of membranes to fibrillation processes and amyloidogenesis.
引用
收藏
页码:372 / 384
页数:13
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