Design of a pH-Dependent Molecular Switch in a Caged Protein Platform

被引：51
|
作者：
Dalmau, Merce [1 ]
Lim, Sierin [1 ]
Wang, Szu-Wen [1 ]
机构：
[1] Univ Calif Irvine, Dept Chem Engn & Mat Sci, Irvine, CA 92697 USA
来源：
NANO LETTERS | 2009年 / 9卷 / 01期
基金：
美国国家科学基金会;
关键词：
BROME MOSAIC-VIRUS; HEAT-SHOCK-PROTEIN; CRYSTALLOGRAPHIC STRUCTURE; CRYOELECTRON MICROSCOPY; MULTIENZYME COMPLEX; CAPSID PROTEIN; DEHYDROGENASE; POLYMORPHISM; PARTICLES; DELIVERY;
D O I：
10.1021/nl8027069
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
Self-assembling protein cages provide a wide range of possible applications in nanotechnology. We report the first example of an engineered pH-dependent molecular switch in a virus-like particle. By genetically manipulating the subunit-subunit interface of the E2 subunit of pyruvate dehydrogenase, we introduce pH-responsive assembly into a scaffold that is natively stable at both pH 5.0 and 7.4. The redesigned protein module yields an intact, stable particle at pH 7.4 that dissociates at pH 5.0. This triggered behavior is especially relevant for applications in therapeutic delivery.
引用
收藏
页码：160 / 166
页数：7
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