Solubilization of phospholipids by detergents structural and kinetic aspects

Dov Lichtenberg, Robert J. Robson, Edward A. Dennis

Research output: Contribution to journalReview articlepeer-review

Abstract

Most amphiphiles in biological membranes including phospholipids, steroids, and membrane proteins are insoluble amphiphiles and would form liquid crystals or insoluble precipitates alone in aqueous media. Detergents are soluble amphiphiles and above a critical concentration and temperature form micelles of various sizes and shapes. Much of the recent progress in studying the insoluble amphiphiles is due to the formation of thermodynamically stable isotropic solutions of these compounds in the presence of detergents. This process, which is commonly denoted as 'solubilization,', involves transformation of lamellar structures into mixed micelles. The information available to date on the solubilization of phospholipids, which constitute the lipid skeleton of biomembranes, by the common detergents is discussed in this review, both with respect to the kinetics of this process and the structure of the various phospholipid-detergent mixed micelles formed. It is hoped that this discussion will lead to somewhat more useful, although still necessarily fairly empirical, approaches to the solubilization of phospholipids by detergents.

Original languageEnglish
Pages (from-to)285-304
Number of pages20
JournalBBA - Reviews on Biomembranes
Volume737
Issue number2
DOIs
StatePublished - 24 May 1983

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