Linked Life Data

20015460

Source:http://linkedlifedata.com/resource/pubmed/id/20015460

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2010-3-12
pubmed:abstractText
Peptidomic analysis of norepinephrine-stimulated skin secretions of the South-East Asian frog Hylarana erythraea (formerly Rana erythraea partim) has led to the identification of multiple peptides with antimicrobial activity. Structural characterization of the peptides demonstrated that they belong to the brevinin-1 (3), brevinin-2 (2), esculentin-2 (4), and temporin (1) families. The values in parentheses indicate the number of paralogs. In addition, a peptide (GVIKSVLKGVAKTVALG ML.NH(2)) was isolated that shows some structural similarity to the brevinin-2-related peptides (B2RP) previously isolated from North American frogs of the genus Lithobates. A synthetic replicate of the species B2RP showed broad-spectrum growth inhibitory activity against reference strains of Escherichia coli (MIC=12.5 microM), Staphylococcus aureus (MIC=12.5 microM) and Candida albicans (MIC=50 microM) and was active against multidrug-resistant clinical isolates of Acetinobacter baumannii (MIC in the range 6-12.5 microM). The hemolytic activity of the peptide was relatively low (LC(50)=280 microM). Phylogenetic analysis based upon the amino acid sequences of 47 brevinin-2 peptides from 17 Asian species belonging to the family Ranidae provides support for the placement of H. erythraea in the genus Hylarana.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1873-5169
pubmed:author
pubmed:copyrightInfo
Copyright (c) 2009 Elsevier Inc. All rights reserved.
pubmed:issnType
Electronic
pubmed:volume
31
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
548-54
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Antimicrobial peptides from the skin secretions of the South-East Asian frog Hylarana erythraea (Ranidae).
pubmed:affiliation
Department of Biochemistry, Faculty of Medicine and Health Sciences, United Arab Emirates University, 17666 Al-Ain, United Arab Emirates.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't