| Revisiting peptide amphiphilicity for membrane pore formation. | |
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MedLine Citation:
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PMID: 21942823 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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It has previously been shown that an amphipathic de novo designed peptide made of 10 leucines and 4 phenylalanines substituted with crown ethers induces vesicle leakage without selectivity. To gain selectivity against negatively charged DMPG bilayers, one or two leucines of the peptide were substituted by positively charged residues at each position. All peptides induce significant calcein leakage of DMPG vesicles. However, some peptides do not induce significant leakage of zwitterionic DMPC vesicles and are thus only active against bacterial model membranes. The intravesicular leakage is induced by pore formation instead of membrane micellization. Non-selective peptides are mostly helical, while selective peptides mainly adopt an intermolecular β-sheet structure. This study therefore demonstrates that the position of the lysine residues significantly influences the secondary structure and bilayer selectivity of an amphipathic 14-mer peptide, with β-sheet peptides being more selective than helical peptides. |
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Authors:
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Aurélien Lorin; Mathieu Noël; Marie-Eve Provencher; Vanessa Turcotte; Carole Masson; Sébastien Cardinal; Patrick Lagüe; Normand Voyer; Michèle Auger |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-9-26 |
Journal Detail:
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Title: Biochemistry Volume: - ISSN: 1520-4995 ISO Abbreviation: - Publication Date: 2011 Sep |
Date Detail:
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Created Date: 2011-9-27 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0370623 Medline TA: Biochemistry Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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