New ganglio-tripod amphiphiles (TPAs) for membrane protein solubilization and stabilization: implications for detergent structure-property relationships
- Authors
- Chae, Pil Seok; Bae, Hyoung Eun; Ehsan, Muhammad; Hussain, Hazrat; Kim, 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.
- Files in This Item
-
Go to Link
- Appears in
Collections - COLLEGE OF ENGINEERING SCIENCES > DEPARTMENT OF BIONANO ENGINEERING > 1. Journal Articles
![qrcode](https://api.qrserver.com/v1/create-qr-code/?size=55x55&data=https://scholarworks.bwise.kr/erica/handle/2021.sw.erica/21140)
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.