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Biochim Biophys Acta. 1998 Nov 10;1376(3):353-68.

Lipid polymorphism and protein-lipid interactions.

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1
Department of Biochemistry, McMaster University Health Sciences Centre, Hamilton, Ont. L8N 3Z5, Canada. epand@fhs.csu.mcmaster.ca

Abstract

Non-lamellar-forming lipids play an important role in determining the physical properties of membranes. They affect the activity of membrane proteins and peptides. In addition, peptides which lyse membranes as well as those which promote membrane fusion facilitate the formation of non-lamellar phases, either micelles, cubic or hexagonal phases. The relationship of these diverse effects on membrane curvature is discussed in relation to the function of certain peptides and proteins. Specific examples of ionophoric peptides, cytotoxic peptides and viral fusion peptides are given. In addition, we compare the modulation of the rate of photoisomerisation of an integral membrane protein, rhodopsin, by non-lamellar-forming lipids with the effects of these lipids on an amphitropic protein, protein kinase C. Among these diverse systems it is frequently observed that the modulation of biological activity can be described in terms of the effect of the peptide or protein on the relative stability of lamellar and non-lamellar structures.

PMID:
9804988
[Indexed for MEDLINE]
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