STABILIZATION OF SECONDARY STRUCTURE OF ALZHEIMER P-PROTEIN BY ALUMINUM(III) IONS AND D-ASP SUBSTITUTIONS

被引：35

作者：

VYAS, SB

DUFFY, LK

机构：

[1] UNIV ALASKA FAIRBANKS,DEPT CHEM & BIOCHEM,FAIRBANKS,AK 99775

[2] UNIV ALASKA FAIRBANKS,INST ARCTIC BIOL,FAIRBANKS,AK 99775

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1995年 / 206卷 / 02期

关键词：

D O I：

10.1006/bbrc.1995.1101

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：

The CD spectra of the D-Asp substituted analogs of amyloid peptides, beta 6-25 and beta 1-40, showed a distinct blue-shift on A1(3+) complexation. The influence of Al3+ coordination was most significant on the triply substituted beta 1-40 (D-Asp (1,7,23)). This analog showed a reduction of the minima near 210nm and a simultaneous increase in the maxima near 200nm as compared to the native L-Asp beta 1-40. These observations suggest that Al3+ interaction with D-Asp induces the peptide backbone to increase its antiparallel beta-sheet character. D-Asp substitution and chelation by A(l3+) lead to increased stability of higher molecular weight species of beta 1-40, and thereby could increase the toxicity of the Alzheimer amyloid protein. (C) 1995 Academic Press, Inc.

引用

页码：718 / 723

页数：6

共 24 条

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