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

Authors
Chae, Pil SeokBae, Hyoung EunEhsan, MuhammadHussain, HazratKim, Jin Woong
Issue Date
Nov-2014
Publisher
Royal Society of Chemistry
Citation
Organic and Biomolecular Chemistry, v.12, no.42, pp.8480 - 8487
Indexed
SCIE
SCOPUS
Journal Title
Organic and Biomolecular Chemistry
Volume
12
Number
42
Start Page
8480
End Page
8487
URI
https://scholarworks.bwise.kr/erica/handle/2021.sw.erica/21140
DOI
10.1039/c4ob01375a
ISSN
1477-0520
Abstract
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.
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COLLEGE OF ENGINEERING SCIENCES > DEPARTMENT OF BIONANO ENGINEERING > 1. Journal Articles

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ERICA 공학대학 (DEPARTMENT OF BIONANO ENGINEERING)
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