Polymorphic phospholipid phase transitions as tools to understand peptide-lipid interactions

• Published in: Chemistry and physics of lipids Vol. 57; no. 2; pp. 327 - 340
• Main Authors: Tournois, H., de Kruijff, B.
• Format: Journal Article
• Language: English
• Published: Shannon Elsevier Ireland Ltd 01.03.1991; Elsevier Science
• Subjects: Amino Acid Sequence; Biological and medical sciences; flip-flop; Fundamental and applied biological sciences. Psychology; fusion; gramicidin; Gramicidin - chemistry; Interactions. Associations; Intermolecular phenomena; Lipid Bilayers - chemistry; lipid polymorphism; Melitten - chemistry; melittin; Membrane Fusion; Membrane Lipids - chemistry; Models, Chemical; Molecular biophysics; Molecular Conformation; Molecular Sequence Data; peptide-lipid interactions; Peptides - chemistry; Phospholipids - chemistry; fusion; DOPE; lipid polymorphism; gramicidin; PC; melittin; IMI; peptide-lipid interactions; PE; flip-flop; DOPC; ILA; Antibiotic; Melittin; Peptides; Structure activity relation; Molecular interaction; Lipids; Artificial membrane; Models; Phase transitions
• ISSN: 0009-3084; 1873-2941
• DOI: 10.1016/0009-3084(91)90084-O

The effect of peptides on bilayer → non-bilayer phase transitions can be used as a tool to investigate the molecular aspects of peptide-lipid interactions. In this contribution the action on membranes of the peptide antibiotic gramicidin A and the bee venom component melittin are compared. Although the know structures and locations of these peptide upon membrane binding are very different, their actions on membranes show striking parallels. A general model is proposed that explains the seemingly complex peptide-lipid interactions by making use of simple concepts.