Lipid reorganization induced by membrane-active peptides probed using differential scanning calorimetry
| Autor: | Solange Lavielle, Sandrine Sagan, Gérard Chassaing, Isabel D. Alves, Chahrazade El Amri, Cécile Galanth, Pierre Nicolas, Pierre Joanne, Nicole Goasdoué |
|---|---|
| Přispěvatelé: | Protéines : biochimie structurale et fonctionnelle (PBSF), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS), Synthèse, Structure et Fonction de Molécules Bioactives (SSFMB), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Université Pierre et Marie Curie - Paris 6 (UPMC), Institut de Médecine Tropicale du Service de Santé des Armées (IMTSSA), Service de Santé des Armées, Laboratoire d'Enzymologie Moléculaire |
| Jazyk: | angličtina |
| Rok vydání: | 2009 |
| Předmět: |
Circular dichroism
Cell Membrane Permeability Protein Conformation Peptide Cell-Penetrating Peptides 01 natural sciences Biochemistry Cricetinae Membrane fluidity Peptide sequence chemistry.chemical_classification 0303 health sciences Membrane active peptide Calorimetry Differential Scanning [CHIM.ORGA]Chemical Sciences/Organic chemistry Peptide–membrane interaction Peptide Conformation lipids (amino acids peptides and proteins) Antimicrobial peptide Cell Survival Antimicrobial peptides Biophysics Nerve Tissue Proteins CHO Cells Microbial Sensitivity Tests 010402 general chemistry Hemolysis Amphibian Proteins Membrane Lipids Structure-Activity Relationship 03 medical and health sciences Cricetulus Differential scanning calorimetry Animals Eye Proteins 030304 developmental biology Cell penetrating peptide Membranes Dermaseptin Cell Biology Lipid lateral reorganization Rats 0104 chemical sciences chemistry Cell-penetrating peptide Carrier Proteins Peptides Antimicrobial Cationic Peptides |
| Zdroj: | BBA-Biochimica et Biophysica Acta BBA-Biochimica et Biophysica Acta, 2009, 1788 ((9):), pp.1772-81. ⟨10.1016/j.bbamem.2009.05.001⟩ BBA-Biochimica et Biophysica Acta, Elsevier, 2009, 1788 ((9):), pp.1772-81. ⟨10.1016/j.bbamem.2009.05.001⟩ |
| ISSN: | 0006-3002 |
| DOI: | 10.1016/j.bbamem.2009.05.001⟩ |
| Popis: | International audience; 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. |
| Databáze: | OpenAIRE |
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