Rational design of a reversible pH-responsive switch for peptide self-assembly

被引：157
|
作者：
Zimenkov, Yuri
Dublin, Steven N.
Ni, Rong
Tu, Raymond S.
Breedveld, Victor
Apkarian, Robert P.
Conticello, Vincent P.
机构：
[1] Emory Univ, Dept Chem, Atlanta, GA 30322 USA
[2] Emory Univ, Integrated Microscopy & Microanalyt Facil, Atlanta, GA 30322 USA
[3] Georgia Inst Technol, Sch Chem & Biomol Engn, Atlanta, GA 30332 USA
来源：
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2006年 / 128卷 / 21期
关键词：
D O I：
10.1021/ja0605974
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
Peptide TZ1H, based on the heptad sequence of a coiled-coil trimer, undergoes fully reversible, pH-dependent self-assembly into long-aspect-ratio helical fibers. Substitution of isoleucine residues with histidine at the core d-positions of alternate heptads introduces a mechanism by which self-assembly is coupled to the protonation state of the imidazole side chain. Circular dichroism spectroscopy, transmission electron microscopy, and microrheology techniques revealed that the self-assembly of TZ1H coincides with a distinct coil-helix conformational transition that occurs within a narrow pH range near the pKa of the imidazole side chains of the core histidine residues. Copyright © 2006 American Chemical Society.
引用
收藏
页码：6770 / 6771
页数：2
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