Surface denaturation and amyloid fibril formation of insulin at model lipid-water interfaces

被引:101
作者
Sharp, JS
Forrest, JA
Jones, RAL
机构
[1] Univ Waterloo, Dept Phys, Waterloo, ON N2L 3G1, Canada
[2] Univ Sheffield, Dept Phys & Astron, Sheffield S3 7RH, S Yorkshire, England
关键词
D O I
10.1021/bi020525z
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
We consider the effects that different lipid surfaces have upon the denaturation and subsequent formation of amyloid fibrils of bovine insulin. The adsorption and unfolding kinetics of insulin being adsorbed onto the different lipid surfaces under denaturing conditions are studied using FTIR ATR spectroscopy and are compared to the bulk solution behavior of the protein. Atomic force microscopy studies are also performed to compare the fibrils growing on the different surfaces. This study shows that both the adsorption and unfolding kinetics of insulin can be described by a sum of exponential processes and that different surfaces behave differently, with respect both to one another and to the bulk protein solution. The proteins adsorbed onto the surfaces are observed to have faster unfolding kinetics than those in the bulk, and the fibril-like structures formed at the surfaces are shown to be different in a number of ways from those found in bulk solution. The beta-sheet content and growth kinetics of the adsorbed proteins also differ from those of the bulk system. An attempt is made to describe the observed behavior in terms of simple physical arguments involving adsorption, unfolding, and aggregation of the proteins.
引用
收藏
页码:15810 / 15819
页数:10
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