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.
