Stabilization of secondary structure of Alzheimer beta-protein by aluminum(III) ions and D-Asp substitutions.
Stabilization of secondary structure of Alzheimer beta-protein by aluminum(III) ions and D-Asp substitutions.
复制标题
通过铝 (III) 离子和 D-Asp 取代稳定阿尔茨海默 β 蛋白的二级结构。
DOI：
10.1006/bbrc.1995.1101
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发表时间：
1995
期刊：
影响因子：
--
通讯作者：
Duffy,LK
中科院分区：
文献类型：
--
作者：
Vyas,SB;Duffy,LK
The CD spectra of the D-Asp substituted analogs of amyloid peptides, β6-25 and β1-40, showed a distinct blue-shift on A13+complexation. The influence of Al3+coordination was most significant on the triply substituted β1-40 (D-Asp1,7,23). 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 β1-40. These observations suggest that Al3+interaction with D-Asp induces the peptide backbone to increase its antiparallel β-sheet character. D-Asp substitution and chelation by Al3+lead to increased stability of higher molecular weight species of β1-40, and thereby could increase the toxicity of the Alzheimer amyloid protein.
