Source:http://linkedlifedata.com/resource/pubmed/id/19254736
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7-8
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pubmed:dateCreated |
2009-5-18
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pubmed:abstractText |
Six structurally similar and strongly cationic peptides belonging to the brevinin-1 family were isolated from skin secretions of the plains leopard frog Lithobates blairi and the lowland leopard frog Lithobates yavapaiensis on the basis of their antimicrobial activities. Brevinin-1BLc (FLPIIAGIAAKFLPKIFCTISKKC) from L. blairi represented the most potent peptide (MIC=25microM Escherichia coli, MIC=1.5microM Staphylococcus aureus, MIC=3microM Candida albicans, LC(50)=9microM human erythrocytes and LC(50)=6microM HepG2 human hepatoma-derived cells). The appreciably lower antimicrobial potencies of brevinin-1Ya and -1Yc from L. yavapaiensis correlate with the decreases in cationicity produced by the amino acid substitutions Lys(11)-->Asn (brevinin-1Ya) and Pro(14)-->Glu (brevinin-1Yc). In addition, a peptide isolated from the skin secretions of L. yavapaiensis belonging to the ranatuerin-2 family (ranatuerin-2Ya; GLMDTIKGVAKTVAASWLDKLKCKIT GC) inhibited the growth of E. coli (MIC=50microM) and S. aureus (MIC=50microM). In contrast to brevinin-1BLc, ranatuerin-2Ya showed appreciably greater cytolytic activity against HepG2 cells (LC(50)=20microM) than against erythrocytes (LC(50)>100microM).
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amphibian Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Anti-Infective Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Antimicrobial Cationic Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Antineoplastic Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/brevinin-1 protein, Rana
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1879-3150
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
53
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
699-705
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pubmed:meshHeading |
pubmed-meshheading:19254736-Amphibian Proteins,
pubmed-meshheading:19254736-Animals,
pubmed-meshheading:19254736-Anti-Infective Agents,
pubmed-meshheading:19254736-Antimicrobial Cationic Peptides,
pubmed-meshheading:19254736-Antineoplastic Agents,
pubmed-meshheading:19254736-Candida albicans,
pubmed-meshheading:19254736-Cell Line,
pubmed-meshheading:19254736-Cell Survival,
pubmed-meshheading:19254736-Chromatography, High Pressure Liquid,
pubmed-meshheading:19254736-Escherichia coli,
pubmed-meshheading:19254736-Humans,
pubmed-meshheading:19254736-Microbial Sensitivity Tests,
pubmed-meshheading:19254736-North America,
pubmed-meshheading:19254736-Peptides,
pubmed-meshheading:19254736-Ranidae,
pubmed-meshheading:19254736-Skin,
pubmed-meshheading:19254736-Staphylococcus aureus
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pubmed:year |
2009
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pubmed:articleTitle |
Peptides with potent cytolytic activity from the skin secretions of the North American leopard frogs, Lithobates blairi and Lithobates yavapaiensis.
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pubmed:affiliation |
Department of Biochemistry, Faculty of Medicine and Health Sciences, United Arab Emirates University, Al-Ain, United Arab Emirates. jmconlon@uaeu.ac.ae
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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