Lipid reorganization induced by membrane-active peptides probed using differential scanning calorimetry

Printer-friendly version
TitleLipid reorganization induced by membrane-active peptides probed using differential scanning calorimetry
Publication TypeJournal Article
Year of Publication2009
AuthorsJoanne P, Galanth C, Goasdoue N, Nicolas P, Sagan S, Lavielle S, Chassaing G, El Amri C, Alves ID
JournalBiochimica Et Biophysica Acta-Biomembranes
Volume1788
Issue9
Pagination1772-1781
Date PublishedSep
ISBN Number0005-2736
Accession NumberISI:000269859400009
Abstract

The overlapping biological behaviors between some cell penetrating peptides (CPPs) and antimicrobial peptides (AMPs) suggest both common and different membrane interaction mechanisms. We thus explore the capacity of selected CPPs and AMPs to reorganize the planar distribution of binary lipid mixtures by means of differential scanning calorimetry (DSC). Additionally, membrane integrity assays and circular dichroism (CD) experiments were performed. Two CPPs (Penetratin and RL16) and AMPs belonging to the dermaseptin superfamily (Drs B2 and C-terminal truncated analog [1-23]-Drs B2 and two plasticins DRP-PBN2 and DRP-PD36KF) were selected. Herein we probed the impact of headgroup charges and acyl chain composition (length and unsaturation) on the peptide/lipid interaction by using binary lipid mixtures. All peptides were shown to be alpha-helical in all the lipid mixtures investigated, except for the two CPPs and [1-23]-Drs B2 in the presence of zwitterionic lipid mixtures where they were rather unstructured. Depending on the lipid composition and peptide sequence, simple binding to the lipid surface that occur without affecting the lipid distribution is observed in particular in the case of AMPs. Recruitments and segregation of lipids were observed, essentially for CPPs, without a clear relationship between peptide conformation and their effect in the lipid lateral organization. Nonetheless, in most cases after initial electrostatic recognition between the peptide charged amino acids and the lipid headgroups, the lipids with the lowest phase transition temperature were selectively recruited by cationic peptides while those with the highest phase transition were segregated. Membrane activities of CPPs and AMPs could be thus related to their preferential interactions with membrane defects that correspond to areas with marked fluidity. Moreover, due to the distinct membrane composition of prokaryotes and eukaryotes, lateral heterogeneity may be differently affected by cationic peptides leading to either uptake or/and antimicrobial activities. (C) 2009 Elsevier B.V. All rights reserved.

URL<Go to ISI>://000269859400009
DOI10.1016/j.bbamem.2009.05.001
Short TitleLipid reorganization induced by membrane-active peptides probed using differential scanning calorimetry
Unit: 
Departement