Gramicidin induced aggregation and size increase of phosphatidylcholine vesicles.
To investigate the role of membrane proteins in the fusion process, linear hydrophobic polypeptide gramicidin was used as fusogenic agent in small unilamellar vesicles (SUV) constituted of saturated lecithins. It was found that gramicidin, externally added to a suspension of vesicles, induces a reversible vesicles aggregation. When incorporated into the bilayer, gramicidin induces increase in vesicle size. The vesicle size increase was monitored by column chromatography and transmission electron microscopy. The process of vesicle size increase occurs only when the lipid membrane is in the gel state. A maximum is observed in the kinetics at a temperature of approx. 25 degrees C lower than the phase transition temperature of lipids. Higher rates of vesicle size increase are obtained as the lipid chain length increases. The process is accompanied by a release of internal vesicle content and by membrane lipid mixing.
Massari
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Colonna
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D001921:Brain; D004134:Dimyristoylphosphatidylcholine; D006096:Gramicidin; D007700:Kinetics; D008051:Lipid Bilayers; D008854:Microscopy, Electron; D008954:Models, Biological; D008968:Molecular Conformation; D010713:Phosphatidylcholines; D010718:Phosphatidylserines; D011663:Pulmonary Surfactants; D013329:Structure-Activity Relationship
D008051:Lipid Bilayers; D010713:Phosphatidylcholines; D010718:Phosphatidylserines; D011663:Pulmonary Surfactants; D006096:Gramicidin; C010942:1,2-distearoyllecithin; D004134:Dimyristoylphosphatidylcholine