Lipid polymorphism and protein-lipid interactions.
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.
Epand
R M
RM
Department of Biochemistry, McMaster University Health Sciences Centre, Hamilton, Ont. L8N 3Z5, Canada. epand@fhs.csu.mcmaster.ca
D000818:Animals; D006096:Gramicidin / Q000737:chemistry; D006801:Humans; D008051:Lipid Bilayers / Q000737:chemistry; D008561:Membrane Fusion; D008563:Membrane Lipids / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry*; D011493:Protein Kinase C / Q000378:metabolism; D012243:Rhodopsin / Q000378:metabolism; D014760:Viral Fusion Proteins / Q000737:chemistry
D008051:Lipid Bilayers; D008563:Membrane Lipids; D008565:Membrane Proteins; D014760:Viral Fusion Proteins; D006096:Gramicidin; D012243:Rhodopsin; D011493:Protein Kinase C