New ganglio-tripod amphiphiles (TPAs) for membrane protein solubilization and stabilization: implications for detergent structure-property relationships

被引:13
|
作者
Chae, Pil Seok [1 ]
Bae, Hyoung Eun [1 ]
Ehsan, Muhammad [1 ]
Hussain, Hazrat [1 ]
Kim, Jin Woong [1 ,2 ]
机构
[1] Hanyang Univ, Dept Bionanotechnol, Ansan 426791, South Korea
[2] Hanyang Univ, Dept Appl Chem, Ansan 426791, South Korea
基金
新加坡国家研究基金会;
关键词
MUSCARINIC ACETYLCHOLINE-RECEPTOR; GLYCOL GNG AMPHIPHILES; CRYSTAL-STRUCTURE; FACIAL AMPHIPHILES; AQUEOUS-SOLUTIONS; COUPLED RECEPTOR; MNG AMPHIPHILES; CRYSTALLIZATION; SURFACTANTS; MANIPULATION;
D O I
10.1039/c4ob01375a
中图分类号
O62 [有机化学];
学科分类号
070303 ; 081704 ;
摘要
Detergents are widely used for membrane protein research; however, membrane proteins encapsulated in micelles formed by conventional detergents tend to undergo structural degradation, necessitating the development of new agents with enhanced efficacy. Here we prepared several hydrophobic variants of ganglio-tripod amphiphiles (TPAs) derived from previously reported TPAs and evaluated for a multi-subunit, pigment protein superassembly. In this study. TPA-16 was found to be most efficient in protein solubilization while TPA-15 proved most favourable in long-term protein stability. The current study combined with previous TPA studies enabled us to elaborate on a few detergent structure-property relationships that could provide useful guidelines for novel amphiphile design.
引用
收藏
页码:8480 / 8487
页数:8
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