Isomeric Detergent Comparison for Membrane Protein Stability: Importance of Inter-Alkyl-Chain Distance and Alkyl Chain Length
Research output: Contribution to journal › Journal article › Research › peer-review
Standard
Isomeric Detergent Comparison for Membrane Protein Stability : Importance of Inter-Alkyl-Chain Distance and Alkyl Chain Length. / Cho, Kyung Ho; Hariharan, Parameswaran; Mortensen, Jonas S.; Du, Yang; Nielsen, Anne K.; Byrne, Bernadette; Kobilka, Brian K.; Loland, Claus J.; Guan, Lan; Chae, Pil Seok.
In: ChemBioChem, Vol. 17, No. 24, 14.12.2016, p. 2334–2339.Research output: Contribution to journal › Journal article › Research › peer-review
Harvard
APA
Vancouver
Author
Bibtex
}
RIS
TY - JOUR
T1 - Isomeric Detergent Comparison for Membrane Protein Stability
T2 - Importance of Inter-Alkyl-Chain Distance and Alkyl Chain Length
AU - Cho, Kyung Ho
AU - Hariharan, Parameswaran
AU - Mortensen, Jonas S.
AU - Du, Yang
AU - Nielsen, Anne K.
AU - Byrne, Bernadette
AU - Kobilka, Brian K.
AU - Loland, Claus J.
AU - Guan, Lan
AU - Chae, Pil Seok
PY - 2016/12/14
Y1 - 2016/12/14
N2 - Membrane proteins encapsulated by detergent micelles are widely used for structural study. Because of their amphipathic property, detergents have the ability to maintain protein solubility and stability in an aqueous medium. However, conventional detergents have serious limitations in their scope and utility, particularly for eukaryotic membrane proteins and membrane protein complexes. Thus, a number of new agents have been devised; some have made significant contributions to membrane protein structural studies. However, few detergent design principles are available. In this study, we prepared meta and ortho isomers of the previously reported para-substituted xylene-linked maltoside amphiphiles (XMAs), along with alkyl chain-length variation. The isomeric XMAs were assessed with three membrane proteins, and the meta isomer with a C12 alkyl chain was most effective at maintaining solubility/stability of the membrane proteins. We propose that interplay between the hydrophile–lipophile balance (HLB) and alkyl chain length is of central importance for high detergent efficacy. In addition, differences in inter-alkyl-chain distance between the isomers influence the ability of the detergents to stabilise membrane proteins.
AB - Membrane proteins encapsulated by detergent micelles are widely used for structural study. Because of their amphipathic property, detergents have the ability to maintain protein solubility and stability in an aqueous medium. However, conventional detergents have serious limitations in their scope and utility, particularly for eukaryotic membrane proteins and membrane protein complexes. Thus, a number of new agents have been devised; some have made significant contributions to membrane protein structural studies. However, few detergent design principles are available. In this study, we prepared meta and ortho isomers of the previously reported para-substituted xylene-linked maltoside amphiphiles (XMAs), along with alkyl chain-length variation. The isomeric XMAs were assessed with three membrane proteins, and the meta isomer with a C12 alkyl chain was most effective at maintaining solubility/stability of the membrane proteins. We propose that interplay between the hydrophile–lipophile balance (HLB) and alkyl chain length is of central importance for high detergent efficacy. In addition, differences in inter-alkyl-chain distance between the isomers influence the ability of the detergents to stabilise membrane proteins.
U2 - 10.1002/cbic.201600429
DO - 10.1002/cbic.201600429
M3 - Journal article
C2 - 27981750
VL - 17
SP - 2334
EP - 2339
JO - ChemBioChem
JF - ChemBioChem
SN - 1439-4227
IS - 24
ER -
ID: 169361980