The influence of proteins and peptides on the phase properties of lipids.
This paper reviews model membrane studies on the modulation of the macroscopic structure of lipids by lipid-protein interactions, with particular emphasis on the gramicidin molecule. This hydrophobic peptide has three main effects on lipid polymorphism: (1) in lysophosphatidylcholine it triggers a micellar to bilayer transition, (2) in phosphatidylethanolamine it lowers the bilayer to hexagonal HII phase transition temperature and (3) in phosphatidylcholine and other bilayer preferring lipids it is able to induce the formation of an HII phase. From experiments in which the gramicidin molecule was chemically modified it can be concluded that the tryptophan residues play a determining role in the peptide-induced changes in polymorphism. The experimental data lead to the proposal that gramicidin molecules have a tendency to self-associate, possibly mediated by tryptophan-tryptophan interactions and organize into tubular structures such as found in the HII phase.
D000595:Amino Acid Sequence; D005614:Freeze Fracturing; D006096:Gramicidin; D008051:Lipid Bilayers; D008244:Lysophosphatidylcholines; D009682:Magnetic Resonance Spectroscopy; D008563:Membrane Lipids / Q000502:physiology; D008565:Membrane Proteins / Q000502:physiology; D008854:Microscopy, Electron; D008954:Models, Biological; D008968:Molecular Conformation; D010455:Peptides / Q000502:physiology; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D013816:Thermodynamics
D008051:Lipid Bilayers; D008244:Lysophosphatidylcholines; D008563:Membrane Lipids; D008565:Membrane Proteins; D010455:Peptides; D006096:Gramicidin