Structural Discrimination between Aβ(1-40) and Aβ(1-42) Peptides in Films with Vibrational Circular Dichroism Spectroscopy

被引：3

作者：

Morisaku, Toshinori ^{[1
]}

Yui, Hiroharu ^{[1
]}

机构：

[1] Tokyo Univ Sci, Dept Chem, Fac Sci, Shinjuku Ku, 1-3 Kagurazaka, Tokyo 1628601, Japan

来源：

ANALYTICAL SCIENCES | 2017年 / 33卷 / 01期

关键词：

A beta; secondary structure; vibrational circular dichroism spectroscopy; beta-sheet; AMYLOID-BETA-PEPTIDE; ALZHEIMERS-DISEASE; IN-VITRO; A-BETA-40; MODEL; NEUROTOXICITY; AGGREGATION; DEPOSITION; TOXICITY; FIBRILS;

D O I：

10.2116/analsci.33.79

中图分类号：

O65 [分析化学];

学科分类号：

070302 ; 081704 ;

摘要：

The secondary structure of full-length A beta(1-40) and. A beta(1-42) peptides in films has been investigated with IR and vibrational circular dichroism (VCD) spectroscopy. From IR spectra, it is shown that the prepared films of A beta(1-40) and A beta(1-42) mainly comprise the beta-sheet conformation that is characteristic of aggregated and fibrous A beta. In the VCD spectra, the A beta(1-42) film shows an intense and sharp band with left-handed optical activity at around 1625 cm(-1), while the A beta(1-40) film shows a weak and broad band with right-handed activity at around 1630 cm(-1). The wavenumbers are characteristic of the beta-sheet conformation. It has been clarified that the aggregated A beta(1-42) adopts the beta-sheet conformation with reverse optical activity compared with the aggregated A beta(1-40). The left-handed optically active beta-sheet of the aggregated A beta(1-42) may contribute to the formation of protofibrils, which are a cause for the higher neurotoxicity of A beta(1-42) fibrils than A beta(1-40) fibrils.

引用

页码：79 / 82

页数：4

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