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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Lavielle, Solange El Amri, Chahrazade Joanne, Pierre Nicolas, Pierre Sagan, Sandrine Alves, Isabel D. Galanth, Cécile Chassaing, Gérard Goasdoué, Nicole |
| Description | Author Affiliation: Joanne P ( UPMC Univ Paris 06, FRE 2852 Peptidome de la Peau d'Amphibiens, Paris F-75005, France.) |
| 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 α-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. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 9 |
| Volume Number | 1788 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2009-09-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Membrane Lipids Chemistry Amphibian Proteins Metabolism Animals Antimicrobial Cationic Peptides CHO Cells Calorimetry, Differential Scanning Carrier Proteins Cell Membrane Permeability Drug Effects Cell Survival Circular Dichroism Cricetinae Cricetulus Eye Proteins Hemolysis Membranes Microbial Sensitivity Tests Nerve Tissue Proteins Peptides Protein Conformation Structure-Activity Relationship Research Support, Non-U.S. Gov't Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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