| Disruption of Saccharomyces cerevisiae by Plantaricin 149 and investigation of its mechanism of action with biomembrane model systems. | |
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MedLine Citation:
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PMID: 19595988 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The action of a synthetic antimicrobial peptide analog of Plantaricin 149 (Pln149a) against Saccharomyces cerevisiae and its interaction with biomembrane model systems were investigated. Pln149a was shown to inhibit S. cerevisiae growth by more than 80% in YPD medium, causing morphological changes in the yeast wall and remaining active and resistant to the yeast proteases even after 24 h of incubation. Different membrane model systems and carbohydrates were employed to better describe the Pln149a interaction with cellular components using circular dichroism and fluorescence spectroscopies, adsorption kinetics and surface elasticity in Langmuir monolayers. These assays showed that Pln149a does not interact with either mono/polysaccharides or zwitterionic LUVs, but is strongly adsorbed to and incorporated into negatively charged surfaces, causing a conformational change in its secondary structure from random-coil to helix upon adsorption. From the concurrent analysis of Pln149a adsorption kinetics and dilatational surface elasticity data, we determined that 2.5 muM is the critical concentration at which Pln149a will disrupt a negative DPPG monolayer. Furthermore, Pln149a exhibited a carpet-like mechanism of action, in which the peptide initially binds to the membrane, covering its surface and acquiring a helical structure that remains associated to the negatively charged phospholipids. After this electrostatic interaction, another peptide region causes a strain in the membrane, promoting its disruption. |
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Authors:
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Jos?? Luiz S Lopes; Thatyane M Nobre; Alvaro Siano; Ver??nica Humpola; Nelma R S Bossolan; Maria E D Zaniquelli; Georgina Tonarelli; Leila M Beltramini |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2009-07-23 |
Journal Detail:
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Title: Biochimica et biophysica acta Volume: 1788 ISSN: 0006-3002 ISO Abbreviation: Biochim. Biophys. Acta Publication Date: 2009 Oct |
Date Detail:
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Created Date: 2009-10-05 Completed Date: 2009-12-22 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0217513 Medline TA: Biochim Biophys Acta Country: Netherlands |
Other Details:
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Languages: eng Pagination: 2252-8 Citation Subset: IM |
Affiliation:
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Biof??sica Molecular Sergio Mascarenhas, Instituto de F??sica de S??o Carlos, Universidade de S??o Paulo, S??o Carlos, SP, Brazil. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Antimicrobial Cationic Peptides
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pharmacology Bacteriocins / pharmacology* Cell Membrane / drug effects*, metabolism Lipid Bilayers / metabolism* Liposomes / metabolism Models, Biological Phospholipids / metabolism* Saccharomyces cerevisiae / drug effects*, growth & development, metabolism Surface Tension |
| Chemical | |
Reg. No./Substance:
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0/Antimicrobial Cationic Peptides; 0/Bacteriocins; 0/Lipid Bilayers; 0/Liposomes; 0/Phospholipids; 0/plantaricin 149 |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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