The Molecular Basis for Antimicrobial Activity of Pore-Forming Cyclic Peptides
dc.contributor.author
dc.date.accessioned
2013-02-19T16:26:58Z
dc.date.available
2013-02-19T16:26:58Z
dc.date.issued
2011
dc.identifier.issn
0006-3495
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dc.description.abstract
The mechanism of action of antimicrobial peptides is, to our knowledge, still poorly understood. To probe the biophysical characteristics that confer activity, we present here a molecular-dynamics and biophysical study of a cyclic antimicrobial peptide and its inactive linear analog. In the simulations, the cyclic peptide caused large perturbations in the bilayer and cooperatively opened a disordered toroidal pore, 1–2 nm in diameter. Electrophysiology measurements confirm discrete poration events of comparable size. We also show that lysine residues aligning parallel to each other in the cyclic but not linear peptide are crucial for function. By employing dual-color fluorescence burst analysis, we show that both peptides are able to fuse/aggregate liposomes but only the cyclic peptide is able to porate them. The results provide detailed insight on the molecular basis of activity of cyclic antimicrobial peptides
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application/pdf
dc.language.iso
eng
dc.publisher
Biophysical Society
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Reproducció digital del document publicat a: http://dx.doi.org/10.1016/j.bpj.2011.03.057
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Biophysical Journal, 2011, vol. 100, núm. 10, p. 2422-2431
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Articles publicats (D-Q)
dc.rights
Attribution-NonCommercial 2.0 Spain
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dc.subject
dc.title
The Molecular Basis for Antimicrobial Activity of Pore-Forming Cyclic Peptides
dc.type
info:eu-repo/semantics/article
dc.rights.accessRights
info:eu-repo/semantics/openAccess
dc.type.version
info:eu-repo/semantics/publishedVersion
dc.identifier.doi
dc.identifier.eissn
1542-0086