Ludwig-Maximilians-Universität, Chair of Metabolic Biochemistry

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Magainin oligomers reversibly dissipate delta microH+ in cytochrome oxidase liposomes

Biochemistry. 1994 Apr 19;33(15):4562-70.

Authors/Editors: Juretić D
Hendler RW
Kamp F
Caughey WS
Zasloff M
Westerhoff HV
Publication Date: 1994
Type of Publication: Journal Article
Magainin peptides present in the skin of Xenopus laevis and identified as antimicrobial agents are shown to decrease the membrane potential in cytochrome oxidase liposomes. They also released respiratory control with a third or higher order concentration dependence. Respiratory control was restored by proteolytic digestion of the added magainin. The amount of magainin required for half-maximal stimulation of respiration was proportional to lipid concentration. At appreciably higher concentrations magainins inhibited uncoupled respiration. The results are discussed in terms of a model in which most of the added magainin adsorbs as a monomer to the membranes but equilibrates with a multimeric pore that causes rather general permeability of membranes. The ensuing ion permeation dissipates membrane potential and stimulates respiration.

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