Magainin 2 amide and analogues Antimicrobial activity, membrane depolarization and susceptibility to proteolysis
- 5 June 1989
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 249 (2), 219-223
- https://doi.org/10.1016/0014-5793(89)80627-1
Abstract
We compared the abilities of synthetic magainin 2 amide and its analogues to inhibit the growth of Escherichia coli and to cause membrane depolarization in E. coli cells and cytochrome oxidase liposomes. The analogue, magainin A, was about 40‐times more active than magainin 2 amide in inhibiting the growth of E. coli and had a much more sustained effect on the membrane potential. In the liposomal system, however, there was only approx. 20% difference between these two peptides in the reduction of membrane potential and uncoupling of respiration. Studies with pronase digestion suggested that the difference in potency may be due to differential susceptibility to proteolysis in the presence of membranes.This publication has 8 references indexed in Scilit:
- Synthetic magainin analogues with improved antimicrobial activityFEBS Letters, 1988
- Antimicrobial properties of peptides from Xenopus granular gland secretionsFEBS Letters, 1988
- Antimicrobial activity of synthetic magainin peptides and several analogues.Proceedings of the National Academy of Sciences, 1988
- Dynamics of proteoliposome formation. Intermediate states during detergent dialysisBiochemical Journal, 1987
- Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor.Proceedings of the National Academy of Sciences, 1987
- Biosynthesis and degradation of peptides derived from Xenopus laevis prohormonesBiochemical Journal, 1987
- Instrumentation and procedures for real time measurements of proton motive force, membrane potential, ΔpH, proton extrusion, and oxygen uptake in respiring cells and vesiclesReview of Scientific Instruments, 1983
- Studies on the Permeability Change Produced in Coliform Bacteria by EthylenediaminetetraacetateJournal of Biological Chemistry, 1968