3,4-Bis(hydroxymethyl)hexane-1,6-diol-based Maltosides (HDMs) for membrane-protein study: importance of detergent rigidity-flexibility balance in protein stability
File(s)
Accepted version
Author(s)
Type
Journal Article
Abstract
Detergents have been major contributors to membrane-protein structural study for decades. However, membrane proteins solubilized in conventional detergents tend to aggregate or denature over time. Stability of large eukaryotic membrane proteins with complex structures tends to be particularly poor, necessitating development of novel detergents with improved properties. Here, we prepared a novel class of detergents, designated 3,4-bis(hydroxymethyl)hexane-1,6-diol-based maltosides (HDMs). When tested on three membrane proteins, including two G-protein-coupled receptors (GPCRs), the new detergents displayed significantly better behaviors compared with DDM. Moreover, the HDMs were superior or comparable to LMNG, an amphiphile widely used for GPCR structural study. An optimal balance of detergent rigidity vs. flexibility of the HDMs is likely responsible for their favorable behaviors toward membrane-protein stability. Thus, the current study not only introduces the HDMs, with significant potential for membrane-protein structural study, but also suggests a useful guideline for designing novel detergents for membrane-protein research.
Date Issued
2022-12-14
Date Acceptance
2022-10-14
Citation
Chemistry: An Asian Journal, 2022, 17 (24)
ISSN
1861-471X
Publisher
Wiley-VCH Verlag
Journal / Book Title
Chemistry: An Asian Journal
Volume
17
Issue
24
Copyright Statement
© 2022 Wiley-VCH GmbH. This is the peer reviewed version of the following article, which has been published in final form at https://onlinelibrary.wiley.com/doi/10.1002/asia.202200941. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions. This article may not be enhanced, enriched or otherwise transformed into a derivative work, without express permission from Wiley or by statutory rights under applicable legislation. Copyright notices must not be removed, obscured or modified. The article must be linked to Wiley’s version of record on Wiley Online Library and any embedding, framing or otherwise making available the article or pages thereof by third parties from platforms, services and websites other than Wiley Online Library must be prohibited.
Identifier
https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000879919500001&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=a2bf6146997ec60c407a63945d4e92bb
Subjects
Science & Technology
Physical Sciences
Chemistry, Multidisciplinary
Chemistry
amphiphiles
membrane proteins
molecular design
HDM
molecular flexibility
BETA(2)-ADRENERGIC RECEPTOR
FACIAL AMPHIPHILES
CRYSTAL-STRUCTURE
GNG AMPHIPHILES
STABILIZATION
CRYSTALLIZATION
SOLUBILIZATION
SURFACTANTS
SYSTEMS
YIELDS
Publication Status
Published
Article Number
ARTN e202200941
Date Publish Online
2022-11-17