MAGAININ OLIGOMERS REVERSIBLY DISSIPATE DELTA-MU(H+) IN CYTOCHROME-OXIDASE LIPOSOMES

被引:41
作者
JURETIC, D
HENDLER, RW
KAMP, F
CAUGHEY, WS
ZASLOFF, M
WESTERHOFF, HV
机构
[1] NHLBI, CELL BIOL LAB, MEMBRANE ENZYMOL SECT, BETHESDA, MD 20892 USA
[2] UNIV AMSTERDAM, BIOCTR, EC SLATER INST BIOCHEM RES, 1018 TV AMSTERDAM, NETHERLANDS
[3] COLORADO STATE UNIV, DEPT BIOCHEM, FT COLLINS, CO 80523 USA
[4] CHILDRENS HOSP PHILADELPHIA, DEPT PEDIAT, PHILADELPHIA, PA 19104 USA
[5] CHILDRENS HOSP PHILADELPHIA, DEPT GENET, DIV HUMAN GENET, PHILADELPHIA, PA 19104 USA
[6] MAGAININ SCI INC, PLYMOUTH MEETING, PA USA
[7] NETHERLANDS CANC INST, DIV MOLEC BIOL, 1066 CX AMSTERDAM, NETHERLANDS
关键词
D O I
10.1021/bi00181a017
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:4562 / 4570
页数:9
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