Allosteric stabilization of the amyloid-β peptide hairpin by the fluctuating N-terminal

被引：22

作者：

Xu, Liang ^{[1
]}

Nussinov, Ruth ^{[2
,3
]}

Ma, Buyong ^{[2
]}

机构：

[1] Dalian Univ Technol, Sch Chem, Dalian, Peoples R China

[2] NCI, Basic Sci Program, Leidos Biomed Res Inc, Canc & Inflammat Program, Frederick, MD 21702 USA

[3] Tel Aviv Univ, Sackler Sch Med, Dept Human Genet & Mol Med, Sackler Inst Mol Med, IL-69978 Tel Aviv, Israel

来源：

CHEMICAL COMMUNICATIONS | 2016年 / 52卷 / 08期

关键词：

ALZHEIMERS-DISEASE; AGGREGATION BEHAVIOR; PROTEIN; MUTATION; MONOMERS; H6R; D7N; SIMULATIONS; MODULATION; OLIGOMERS;

D O I：

10.1039/c5cc08107f

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Immobilized ions modulate nearby hydrophobic interactions and influence molecular recognition and self-assembly. We simulated disulfide bond-locked double mutants (L17C/L34C) and observed allosteric modulation of the peptide's intra-molecular interactions by the N-terminal tail. We revealed that the non-contacting charged N-terminal residues help the transfer of entropy to the surrounding solvation shell and stabilizing beta-hairpin.

引用

页码：1733 / 1736

页数：4

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