Interfacial Effects on the Conformation of Amyloid-Beta Peptide

被引：2

作者：

Seidler, Norbert W. ^{[1
]}

Eklund, Joshua D. ^{[1
]}

机构：

[1] Kansas City Univ Med & Biosci, Dept Biochem, Kansas City, MO 64106 USA

来源：

PROTEIN AND PEPTIDE LETTERS | 2009年 / 16卷 / 02期

关键词：

Amyloid-beta; interface; sevoflurane; fluorescence; protein folding; AIR-WATER-INTERFACE; ALZHEIMERS-DISEASE; BINDING; POLYACROLEIN; FLUORESCENCE; ASSOCIATION; MECHANISM; PRESSURE; LYSOZYME; SERUM;

D O I：

10.2174/092986609787316324

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 examined the effects of air-water and water-sevoflurane interfaces on conformational properties of amyloid-beta peptide (ABP). Fractions were extracted from sub-interfacial (air-water) and supra-interfacial (water-sevoflurane) layers and compared with aqueous bulk layers using fluorescence properties of ABP provided by a single tyrosine. The observations suggest that interfacial ABP may be more disordered than bulk ABP.

引用

页码：182 / 188

页数：7

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