pH changes the aggregation propensity of amyloid-β without altering the monomer conformation

被引：27

作者：

Bhowmik, Debanjan ^{[1
]}

MacLaughlin, Christina M. ^{[2
]}

Chandrakesan, Muralidharan ^{[3
,4
]}

Ramesh, Prashanth ^{[1
]}

Venkatramani, Ravindra ^{[1
]}

Walker, Gilbert C. ^{[2
]}

Maiti, Sudipta ^{[1
]}

机构：

[1] Tata Inst Fundamental Res, Dept Chem, Mumbai 400005, Maharashtra, India

[2] Univ Toronto, Lash Miller Labs, Dept Chem, Toronto, ON M5S 3H6, Canada

[3] Seth GS Med Coll, Dept Biochem, Bombay 400012, Maharashtra, India

[4] King Edward Mem Hosp, Bombay 400012, Maharashtra, India

来源：

PHYSICAL CHEMISTRY CHEMICAL PHYSICS | 2014年 / 16卷 / 03期

关键词：

DISCRETE MOLECULAR-DYNAMICS; ALZHEIMERS-DISEASE; LYSOSOMAL MEMBRANE; RAMAN-SPECTROSCOPY; PRECURSOR PROTEIN; IN-VIVO; FIBRILS; PEPTIDE; OLIGOMERS; A-BETA(1-40);

D O I：

10.1039/c3cp54151g

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

Decoupling conformational changes from aggregation will help us understand amyloids better. Here we attach Alzheimer's amyloid-beta(1-40) monomers to silver nanoparticles, preventing their aggregation, and study their conformation under aggregation-favoring conditions using SERS. Surprisingly, the alpha-helical character of the peptide remains unchanged between pH 10.5 and 5.5, while the solubility changes >100X. Amyloid aggregation can therefore start without significant conformational changes.

引用

页码：885 / 889

页数：5

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