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Publication Details
AFRICAN RESEARCH NEXUS
SHINING A SPOTLIGHT ON AFRICAN RESEARCH
Solution structure and model membrane interactions of temporins-SH, antimicrobial peptides from amphibian skin. A NMR spectroscopy and differential scanning calorimetry study
Biochemistry, Volume 47, No. 40, Year 2008
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Description
Temporin-SHa and temporin-SHc are 13 residue long antimicrobial peptides from frog skin that have similar sequences but differ markedly in their membrane-damaging properties. Temporin-SHa contains a single basic lysine residue and has a unique antimicrobial spectrum of action among temporins, being very potent against Gram-positive and Gram-negative bacteria, yeasts, fungi, and protozoa. Temporin-SHc, which contains a single basic histidine residue, is inactive against Gram-negative bacteria, has a reduced efficacy against Gram-positive bacteria, but is still active against yeasts and fungi. Temporin-SHb, with no basic residue, has no antimicrobial activity. The three-dimensional structures of the peptides bound to SDS micelles were analyzed by CD and NMR spectroscopy combined with restrained molecular dynamics calculations. The peptides adopt well-defined amphipathic α-helical structures extending from residue 3 to residue 12, when bound to SDS micelles. The structures are stabilized by extensive interactions between aliphatic and aromatic side chains on the nonpolar face. Relaxation enhancements caused by paramagnetic probes showed that the peptides adopt nearly parallel orientations to the micelle surface and do not deeply penetrate into the micelle. The interaction of the peptides with model membranes was investigated by differential scanning calorimetry on anionic and zwitterionic multilamellar vesicles and membrane-permeabilization assays on calcein-loaded large unilamellar vesicles. Calorimetric data indicated that both temporin-SHa and -SHc reside at the hydrocarbon core-water interface of the anionic lipid bilayer but interact with anionic bilayers in a very different manner. This suggests that the charge-induced activity of temporins-SH for bacterial cells is due to changes in the membrane-disturbing mechanism of the bound peptides. © 2008 American Chemical Society.
Authors & Co-Authors
Abbassi, Feten
France, Paris
Sorbonne Université
Tunisia, Sousse
Faculty of Medicine Sousse
Galanth, Cécile
France, Paris
Sorbonne Université
Amiche, Mohamed
France, Paris
Sorbonne Université
Saito, Kazuko
France, Paris
Sorbonne Université
Piesse, Christophe
France, Paris
Sorbonne Université
Zargarian, Loussinée
France, Cachan
Laboratoire de Biologie et Pharmacologie Appliquée
Hani, Khaled
Tunisia, Sousse
Faculty of Medicine Sousse
Nicolas, Pierre
France, Paris
Sorbonne Université
Lequin, Olivier
France, Paris
Sorbonne Université
Ladram, Ali
France, Paris
Sorbonne Université
Statistics
Citations: 42
Authors: 10
Affiliations: 3
Identifiers
Doi:
10.1021/bi8006884
Research Areas
Environmental