Linked Life Data

21575576

Source:http://linkedlifedata.com/resource/pubmed/id/21575576

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2011-5-17
pubmed:abstractText
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1542-0086
pubmed:author
pubmed:copyrightInfo
Copyright © 2011 Biophysical Society. Published by Elsevier Inc. All rights reserved.
pubmed:issnType
Electronic
pubmed:day
18
pubmed:volume
100
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2422-31
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
The molecular basis for antimicrobial activity of pore-forming cyclic peptides.
pubmed:affiliation
Department of Biochemistry and Biophysical Chemistry, Groningen Biomolecular Sciences, Netherlands.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't