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Isomeric Detergent Comparison for Membrane Protein Stability: Importance of Inter-Alkyl-Chain Distance and Alkyl Chain Length

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

  • Kyung Ho Cho
  • Parameswaran Hariharan
  • Jonas S. Mortensen
  • Yang Du
  • Anne K. Nielsen
  • Bernadette Byrne
  • Brian K. Kobilka
  • Løland, Claus Juul
  • Lan Guan
  • Pil Seok Chae
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.
OriginalsprogEngelsk
TidsskriftChemBioChem
Vol/bind17
Udgave nummer24
Sider (fra-til)2334–2339
ISSN1439-4227
DOI
StatusUdgivet - 14 dec. 2016

ID: 169361980