Interaction of an antimicrobial peptide with a model lipid bilayer using molecular dynamics simulation
We present results of molecular dynamics simulations of the interaction of a positively charged antimicrobial peptide, carnobacteriocin B2, with a mixed (anionic-zwitterionic) lipid bilayer carrying a net negative charge. When the peptide is initially immersed in an aqueous medium, it approaches the...
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1992. - 25(2009), 12 vom: 16. Juni, Seite 6591-5 |
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| Weitere Verfasser: | , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2009
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| Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Anti-Infective Agents Bacteriocins Lipid Bilayers Peptides bacteriocin B2 protein, Carnobacterium piscicola 155982-38-0 |
| Zusammenfassung: | We present results of molecular dynamics simulations of the interaction of a positively charged antimicrobial peptide, carnobacteriocin B2, with a mixed (anionic-zwitterionic) lipid bilayer carrying a net negative charge. When the peptide is initially immersed in an aqueous medium, it approaches the bilayer surface because of electrostatic attraction. Insertion of the single peptide in the bilayer, however, is not spontaneous. Simulations are also conducted by employing initial configurations where the peptide is partially or completely inserted into the bilayer. When the peptide is partially inserted into the bilayer, it experiences a slight loss of helical structure with the appearance of a hinge region in the C-terminal helix. Complete insertion of the peptide in the bilayer results in a stable straight helix with the N- and C-terminals electrostatically tethered to the opposing headgroups of the bilayer. The charged amino acids of the peptide do not cross the charged headgroups of the bilayer in any of the simulations, nor is any bilayer disruption observed in these studies. These results show that single peptides do not spontaneously penetrate lipid membranes and corroborate deductions from previous experimental studies that alternate mechanisms are necessary for their penetration into lipid bilayers |
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| Beschreibung: | Date Completed 17.08.2009 Date Revised 09.06.2009 published: Print Citation Status MEDLINE |
| ISSN: | 1520-5827 |
| DOI: | 10.1021/la900365g |