Investigating the role of GXXXG motifs in helical folding and self-association of plasticins, Gly/Leu-rich antimicrobial peptides. - CNRS - Centre national de la recherche scientifique Accéder directement au contenu
Article Dans Une Revue Biophysical Chemistry Année : 2014

Investigating the role of GXXXG motifs in helical folding and self-association of plasticins, Gly/Leu-rich antimicrobial peptides.

Résumé

: Plasticins (PTC) are dermaseptin-related antimicrobial peptides characterized by a large number of leucine and glycine residues arranged in GXXXG motifs that are often described to promote helix association within biological membranes. We report the structure and interaction properties of two plasticins, PTC-B1 from Phyllomedusa bicolor and a cationic analog of PTC-DA1 from Pachymedusa dacnicolor, which exhibit membrane-lytic activities on a broad range of microorganisms. Despite a high number of glycine, CD and NMR spectroscopy show that the two plasticins adopt mainly alpha-helical conformations in a wide variety of environments such as trifluoroethanol, detergent micelles and lipid vesicles. In DPC and SDS, plasticins adopt well-defined helices that lie parallel to the micelle surface, all glycine residues being located on the solvent-exposed face. Spectroscopic data and cross-linking experiments indicate that the GXXXG repeats in these amphipathic helices do not provide a strong oligomerization interface, suggesting a different role from GXXXG motifs found in transmembrane helices.

Domaines

Chimie organique
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Dates et versions

hal-01072550 , version 1 (08-10-2014)

Identifiants

Citer

Ludovic Carlier, Pierre Joanne, Lucie Khemtémourian, Claire Lacombe, Pierre Nicolas, et al.. Investigating the role of GXXXG motifs in helical folding and self-association of plasticins, Gly/Leu-rich antimicrobial peptides.. Biophysical Chemistry, 2014, 196C, pp.40-52. ⟨10.1016/j.bpc.2014.09.004⟩. ⟨hal-01072550⟩
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