On some physicochemical properties of sucrose esters and the stability they confer to membrane proteins

Daniel Abran, François Boucher, Toshiaki Hamanaka, Kenji Hiraki, Yuji Kito, Kenzou Koyama, Roger M. Leblanc, Hazime Machida, Gaétan Munger, Masatsugu Seidou, Michel Tessier

Research output: Contribution to journalArticlepeer-review

20 Scopus citations

Abstract

A homologous series of fatty acid monoesters of sucrose whose chain length varies from 8 to 22 carbon atoms has been examined with respect to some physicochemical properties. In this series, the critical micelle concentration is comparable to that of lysophospholipids having similar hydrophobic moiety. The behavior of a spin probe dispersed in micelles of sucrose esters and their surface pressure-area isotherms at the air/water interface indicate that, despite a relatively large hydrophilic head, they form increasingly compact structures as their chain length increases. Finally, when used as dispersing medium for the purified intrinsic protein rhodopsin, long-chain esters confer to the pigment a thermal stability which is close to that of its membrane-bound state. We conclude that these detergents may be among those best suited to purified intrinsic membrane protein studies.

Original languageEnglish (US)
Pages (from-to)230-236
Number of pages7
JournalJournal of Colloid And Interface Science
Volume128
Issue number1
DOIs
StatePublished - Mar 1 1989

ASJC Scopus subject areas

  • Electronic, Optical and Magnetic Materials
  • Biomaterials
  • Surfaces, Coatings and Films
  • Colloid and Surface Chemistry

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