Das, Manoj K and Balaram, P (1984) Interactions of the channel forming peptide alamethicin with artificial and natural membranes. In: Journal of Biosciences, 6 (4). pp. 337-348.
Alamethicin and related a-aminoisobutyric acid peptides form transmembrane channels across lipid bilayers. This article briefly reviews studies on the effect of alamethicin on lipid phase transitions in lipid bilayers and on mitochondrial oxidative phosphorylation. Fluorescence polarization studies, employing 1,6-diphenyl-1,3,5-hexatriene as a probe, suggest that alamethicin fluidizes lipid bilayers below the phase transition temperature, but has little effect above the gel-liquid crystal transition point. Alamethicin is shown to function as an uncoupler of oxidative phosphorylation in rat liver mitochondria. The influence of alamethicin on mitochondrial respiration is modulated by the phosphate ion concentration in the medium. Classical uncoupling activity is evident at low phosphate levels while inhibitory effects set in at higher phosphate concentrations. Time-dependent changes in respiration rates following peptide addition are rationalized in terms of alamethicin interactions with mitochondrial membrane components.
|Item Type:||Journal Article|
|Additional Information:||Copyright for this article belongs to Indian Academy of Sciences.|
|Keywords:||Alamethicin;membrane channels;mitochondrial uncouplers;mitochondrial in-hibitors;peptide-lipid interactions;membranes|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||07 Mar 2005|
|Last Modified:||19 Sep 2010 04:18|
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