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

Abstract：

: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.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Sharp JS,Forrest JA,Jones RA

doi

10.1021/bi020525z

subject

Has Abstract

pub_date

2002-12-31 00:00:00

pages

15810-9

issue

52

eissn

0006-2960

issn

1520-4995

pii

bi020525z

journal_volume

41

pub_type

杂志文章

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