Insights into the Mechanisms of Amyloid Formation of ZnII-Ab11-28: pH-Dependent Zinc Coordination and Overall Charge as Key Parameters for Kinetics and the Structure of ZnII-Ab11-28 Aggregates

被引：11

作者：

Alies, Bruno ^{[1
,2
]}

LaPenna, Giovanni ^{[3
]}

Sayen, Stephanie ^{[4
]}

Guillon, Emmanuel ^{[4
]}

Hureau, Christelle ^{[1
,2
]}

Faller, Peter ^{[1
,2
]}

机构：

[1] CNRS, LCC, F-31077 Toulouse 4, France

[2] Univ Toulouse, UPS, INPT, F-31077 Toulouse 4, France

[3] CNR Natl Res Council Italy, ICCOM, I-50019 Florence, Italy

[4] Univ Reims, Grp Chim Coordinat, Inst Chim Mol Reims, ICMR,CNRS,UMR 7312, F-51687 Reims 2, France

来源：

INORGANIC CHEMISTRY | 2012年 / 51卷 / 14期

关键词：

MOLECULAR-DYNAMICS; METAL-IONS; ALZHEIMERS-DISEASE; MODEL PEPTIDES; BETA; BINDING; FIBRILS; OLIGOMERIZATION; NANOSTRUCTURES; DISORDERS;

D O I：

10.1021/ic300972j

中图分类号：

O61 [无机化学];

学科分类号：

070301 [无机化学];

摘要：

Self-assembly of amyloidogenic peptides and their metal complexes are of multiple interest including their association with several neurological diseases. Therefore, a better understanding of the role of metal ions in the aggregation process is of broad interest. We report pH-dependent structural and aggregation studies on Zn-II binding to the amyloidogenic peptide Ab11-28. The results suuest that coordination of the N-terminal amine to Zn-II is responsible for the inhibition of amyloid formation and the overall charge for amorphous aggregates.

引用

页码：7897 / 7902

页数：6

共 50 条

[1]

Dynamics of ZnII Binding as a Key Feature in the Formation of Amyloid Fibrils by Aβ11-28 [J].