Linked Life Data

20180000

Source:http://linkedlifedata.com/resource/pubmed/id/20180000

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2010-4-8
pubmed:abstractText
Little is known on antimicrobial peptide permeation through outer membrane channels in gram-negative bacteria. Herein, we probed at a single-molecule level the interaction of two different peptides, magainin 2 and HPA3P with OmpF from E. coli. HPA3P is an analogue of the antimicrobial peptide HP(2-20) isolated from the N-terminal region of the Helicobacter pylori ribosomal protein. Our data show that the shorter and more charged HPA3P peptide is more accessible to the inner volume of the OmpF than magainin 2. We demonstrate the ability of HPA3P peptides to interact with OmpF in a voltage- and concentration-dependent manner, which does not rule out a novel mechanism by which such peptides could reach the periplasmic space of gram-negative bacteria. Unexpectedly, we found that increasing the applied voltage led to an increase of the residence time of HPA3P peptide inside the pore, possibly reflecting electric field-induced changes in pore and peptide geometry.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1573-6881
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
42
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
173-80
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Unimolecular study of the interaction between the outer membrane protein OmpF from E. coli and an analogue of the HP(2-20) antimicrobial peptide.
pubmed:affiliation
Faculty of Physics, Laboratory of Biophysics and Medical Physics, Alexandru I. Cuza' University, Blvd. Carol I, No. 11, Iasi, 700506, Romania.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't