Mesitylene-Cored Glucoside Amphiphiles (MGAs) for Membrane Protein Studies: Importance of Alkyl Chain Density in Detergent Efficacy
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Mesitylene-Cored Glucoside Amphiphiles (MGAs) for Membrane Protein Studies: Importance of Alkyl Chain Density in Detergent Efficacy. / Cho, Kyung Ho; Ribeiro, Orquidea; Du, Yang; Tikhonova, Elena; Mortensen, Jonas; Markham, Kelsey; Hariharan, Parameswaran; Løland, Claus; Guan, Lan; Kobilka, Brian; Byrne, Bernadette; Chae, Pil Seok.
In: Chemistry: A European Journal, Vol. 22, No. 52, 23.12.2016, p. 18833–18839.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Mesitylene-Cored Glucoside Amphiphiles (MGAs) for Membrane Protein Studies: Importance of Alkyl Chain Density in Detergent Efficacy
AU - Cho, Kyung Ho
AU - Ribeiro, Orquidea
AU - Du, Yang
AU - Tikhonova, Elena
AU - Mortensen, Jonas
AU - Markham, Kelsey
AU - Hariharan, Parameswaran
AU - Løland, Claus
AU - Guan, Lan
AU - Kobilka, Brian
AU - Byrne, Bernadette
AU - Chae, Pil Seok
N1 - © 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
PY - 2016/12/23
Y1 - 2016/12/23
N2 - Detergents serve as useful tools for membrane protein structural and functional studies. Their amphipathic nature allows detergents to associate with the hydrophobic regions of membrane proteins whilst maintaining the proteins in aqueous solution. However, widely used conventional detergents are limited in their ability to maintain the structural integrity of membrane proteins and thus there are major efforts underway to develop novel agents with improved properties. We prepared mesitylene-cored glucoside amphiphiles (MGAs) with three alkyl chains and compared these agents with previously developed xylene-linked maltoside agents (XMAs) with two alkyl chains and a conventional detergent (DDM). When these agents were evaluated for four membrane proteins including a G protein-coupled receptor (GPCR), some agents such as MGA-C13 and MGA-C14 resulted in markedly enhanced stability of membrane proteins compared to both DDM and the XMAs. This favourable behaviour is due likely to the increased hydrophobic density provided by the extra alkyl chain. Thus, this study not only describes new glucoside agents with potential for membrane protein research, but also introduces a new detergent design principle for future development.
AB - Detergents serve as useful tools for membrane protein structural and functional studies. Their amphipathic nature allows detergents to associate with the hydrophobic regions of membrane proteins whilst maintaining the proteins in aqueous solution. However, widely used conventional detergents are limited in their ability to maintain the structural integrity of membrane proteins and thus there are major efforts underway to develop novel agents with improved properties. We prepared mesitylene-cored glucoside amphiphiles (MGAs) with three alkyl chains and compared these agents with previously developed xylene-linked maltoside agents (XMAs) with two alkyl chains and a conventional detergent (DDM). When these agents were evaluated for four membrane proteins including a G protein-coupled receptor (GPCR), some agents such as MGA-C13 and MGA-C14 resulted in markedly enhanced stability of membrane proteins compared to both DDM and the XMAs. This favourable behaviour is due likely to the increased hydrophobic density provided by the extra alkyl chain. Thus, this study not only describes new glucoside agents with potential for membrane protein research, but also introduces a new detergent design principle for future development.
U2 - 10.1002/chem.201603338
DO - 10.1002/chem.201603338
M3 - Journal article
C2 - 27743406
VL - 22
SP - 18833
EP - 18839
JO - Chemistry: A European Journal
JF - Chemistry: A European Journal
SN - 0947-6539
IS - 52
ER -
ID: 167933153