The role of histidines in amyloid β fibril assembly

被引：37

作者：

Brannstrom, Kristoffer ^{[1
]}

Islam, Tohidul ^{[1
]}

Sandblad, Linda ^{[2
]}

Olofsson, Anders ^{[1
]}

机构：

[1] Umea Univ, Dept Med Biochem & Biophys, SE-90187 Umea, Sweden

[2] Umea Univ, Dept Mol Biol, Umea, Sweden

来源：

FEBS LETTERS | 2017年 / 591卷 / 08期

基金：

瑞典研究理事会;

关键词：

abeta; amyloid; fibril; histidine; stability; surface plasmon resonance; FAMILIAL ALZHEIMERS-DISEASE; SURFACE-PLASMON RESONANCE; DOCK-LOCK MECHANISM; PEPTIDE; AGGREGATION; PROTEIN; STABILITY; OLIGOMERS; BINDING; BRAIN;

D O I：

10.1002/1873-3468.12616

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：

Low pH has a strong stabilising effect on the fibrillar assembly of amyloid beta, which is associated with Alzheimer's disease. The stabilising effect is already pronounced at pH 6.0, suggesting that protonation of histidines might mediate this effect. Through the systematic substitution of the three native histidines in Ab for alanines, we have evaluated their role in fibril stability. Using surface plasmon resonance, we show that at neutral pH the fibrillar forms of all His-Ala variants are destabilised by a factor of 4-12 compared to wildtype A beta. However, none of the His-Ala Ab variants impair the stabilising effect of the fibril at low pH.

引用

页码：1167 / 1175

页数：9

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