The Cu(II) complex of Aβ40 peptide in ammonium acetate solutions. Evidence for ternary species formation

被引：28

作者：

Rozga, Malgorzata ^{[1
]}

Protas, Anna M. ^{[1
]}

Jablonowska, Agnieszka ^{[1
]}

Dadlez, Michal ^{[1
,2
]}

Bal, Wojciech ^{[1
,3
]}

机构：

[1] Polish Acad Sci, Inst Biochem & Biophys, PL-02106 Warsaw, Poland

[2] Univ Warsaw, Inst Genet & Biotechnol, PL-02106 Warsaw, Poland

[3] Natl Res Inst, Cent Inst Labour Protect, PL-00701 Warsaw, Poland

来源：

CHEMICAL COMMUNICATIONS | 2009年 / 11期

关键词：

AMYLOID-BETA-PEPTIDE; HUMAN-SERUM-ALBUMIN; BINDING-SITE; A-BETA; COPPER(II); ALZHEIMERS; IONS; FRAGMENTS; CONSTANT; ZINC(II);

D O I：

10.1039/b819616h

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Fluorimetric Cu(II) titrations of Alzheimer's disease (AD) A beta 40 peptide at various ammonium acetate concentrations demonstrated that ternary Cu(A beta 40) L complexes are formed with buffer components L, thereby providing a novel perspective on Cu(II)-A beta interactions.

引用

页码：1374 / 1376

页数：3

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