연구진흥

창의적인 신지식 창출과 산업계와의 협력적 네트워크 구축

금주의 우수논문

SCI-E Article; Early Access
Development of 1,3-acetonedicarboxylate-derived glucoside amphiphiles (ACAs) for membrane protein study
채필석
  1. 성명
    채필석
  2. 소속
    공학대학 생명나노공학과
  3. 캠퍼스
  4. 우수선정주
    2022년 05월 2째주
Author
Lee, Ho Jin (Dept Bionano Engn); Ehsan, Muhammad (Dept Bionano Engn); Ahmed, Waqar (Dept Bionano Engn); Kumar, Ashwani (Dept Bionano Engn); 채필석 (Dept Bionano Engn) corresponding author;
Corresponding Author Info
Chae, PS(해당 저자), Hanyang Univ, Dept Bionano Engn, Ansan 15588, South Korea.
E-mail
이메일pchae@hanyang.ac.kr
Document Type
Article; Early Access
Source
CHEMICAL SCIENCE Volume: Issue: Pages:- Published:
Times Cited
0
External Information
http://dx.doi.org/10.1039/d2sc00539e
Abstract
Detergents are extensively used for membrane protein manipulation. Membrane proteins solubilized in conventional detergents are prone to denaturation and aggregation, rendering downstream characterization of these bio-macromolecules difficult. Although many amphiphiles have been developed to overcome the limited efficacy of conventional detergents for protein stabilization, only a handful of novel detergents have so far proved useful for membrane protein structural studies. Here, we introduce 1,3-acetonedicarboxylate-derived amphiphiles (ACAs) containing three glucose units and two alkyl chains as head and tail groups, respectively. The ACAs incorporate two different patterns of alkyl chain attachment to the core detergent unit, generating two sets of amphiphiles: ACA-As (asymmetrically alkylated) and ACA-Ss (symmetrically alkylated). The difference in the attachment pattern of the detergent alkyl chains resulted in minor variation in detergent properties such as micelle size, critical micelle concentration, and detergent behaviors toward membrane protein extraction and stabilization. In contrast, the impact of the detergent alkyl chain length on protein stability was marked. The two C11 variants (ACA-AC11 and ACA-SC11) were most effective at stabilizing the tested membrane proteins. The current study not only introduces new glucosides as tools for membrane protein study, but also provides detergent structure-property relationships important for future design of novel amphiphiles.
Web of Science Categories
Chemistry, Multidisciplinary
Funding
National Research Foundation of Korea (NRF)National Research Foundation of Korea [2021R1A2C2006067, 2018R1A6A1A03024231]; National Institutes of HealthUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USA [R01GM12275
Language
English
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