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Resorcinarene‐Based Facial Glycosides: Implication of Detergent Flexibility on Membrane‐Protein Stability
Author(s) -
Hussain Hazrat,
Du Yang,
Tikhonova Elena,
Mortensen Jonas S.,
Ribeiro Orquidea,
Santillan Claudia,
Das Manabendra,
Ehsan Muhammad,
Loland Claus J.,
Guan Lan,
Kobilka Brian K.,
Byrne Bernadette,
Chae Pil Seok
Publication year - 2017
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201605016
Subject(s) - resorcinarene , amphiphile , chemistry , membrane , micelle , solubility , membrane protein , alkyl , chromatography , aqueous solution , organic chemistry , biochemistry , molecule , copolymer , polymer
As a membrane‐mimetic system, detergent micelles are popularly used to extract membrane proteins from lipid environments and to maintain their solubility and stability in an aqueous medium. However, many membrane proteins encapsulated in conventional detergents tend to undergo structural degradation during extraction and purification, thus necessitating the development of new agents with enhanced properties. In the current study, two classes of new amphiphiles are introduced, resorcinarene‐based glucoside and maltoside amphiphiles (designated RGAs and RMAs, respectively), for which the alkyl chains are facially segregated from the carbohydrate head groups. Of these facial amphiphiles, two RGAs (RGA‐C11 and RGA‐C13) conferred markedly enhanced stability to four tested membrane proteins compared to a gold‐standard conventional detergent. The relatively high water solubility and micellar stability of the RGAs compared to the RMAs, along with their generally favourable behaviours for membrane protein stabilisation described here, are likely to be, at least in part, a result of the high conformational flexibility of these glucosides. This study suggests that flexibility could be an important factor in determining the suitability of new detergents for membrane protein studies.