Antimicrobial peptides from the skin of the Tsushima brown frog Rana tsushimensis

The Tsushima brown frog Rana tsushimensis Stejneger, 1907 exists in reproductive isolation on the island of Tsushima, Japan. Six peptides with antimicrobial activity were isolated in pure form from an extract of the skin of this species and their amino acid sequences identified them as members of th...

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Vydáno v:	Comparative biochemistry and physiology. Toxicology & pharmacology Ročník 143; číslo 1; s. 42 - 49
Hlavní autoři:	Conlon, J. Michael, Al-Ghaferi, Nadia, Abraham, Bency, Sonnevend, Agnes, Coquet, Laurent, Leprince, Jérôme, Jouenne, Thierry, Vaudry, Hubert, Iwamuro, Shawichi
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	United States Elsevier Inc 01.05.2006 Elsevier
Témata:	Amino Acid Sequence Animals Antimicrobial Cationic Peptides Antimicrobial Cationic Peptides - analysis Antimicrobial Cationic Peptides - chemistry Antimicrobial Cationic Peptides - genetics Antimicrobial Cationic Peptides - isolation & purification Antimicrobial Cationic Peptides - pharmacology Antimicrobial peptide Brevinin-1 Brevinin-2 Cell Behavior Cellular Biology Chemical Sciences Conserved Sequence Drug Resistance, Microbial Drug Resistance, Microbial - genetics Female Frog skin Hemolysis Hemolysis - drug effects HPLC purification Humans Life Sciences Medicinal Chemistry Methicillin Resistance Methicillin Resistance - genetics Microbial Sensitivity Tests Molecular Sequence Data Molecular Weight Neurobiology Neurons and Cognition Pharmaceutical sciences Pharmacology Rana Rana okinavana Ranidae Sequence Homology, Amino Acid Skin Skin - chemistry Skin - metabolism Staphylococcus aureus Temporin HPLC purification Brevinin-2 Temporin Brevinin-1 Frog skin Antimicrobial peptide
ISSN:	1532-0456, 1878-1659
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Shrnutí:	The Tsushima brown frog Rana tsushimensis Stejneger, 1907 exists in reproductive isolation on the island of Tsushima, Japan. Six peptides with antimicrobial activity were isolated in pure form from an extract of the skin of this species and their amino acid sequences identified them as members of the brevinin-1 (one peptide), brevinin-2 (one peptide) and temporin (four peptides) families. The C-terminally α-amidated brevinin-1 peptide (FLGSIVGALASALPSLISKIRN.NH 2) lacks the cyclic heptapeptide domain Cys 18–(Xaa) 4–Lys–Cys 24 at the COOH-terminus of the molecule that characterizes other members of that family. A structurally similar brevinin-1 peptide, also lacking the cyclic domain, was previously isolated from the skin of the Ryukyu brown frog Rana okinavana, indicative of a close phylogenetic relationship between the species. Brevinin-2TSa (GIMSLFKGVLKTAGKHVAGSLVDQLKCKITGGC) showed broad-spectrum growth inhibitory activity against a range of Gram-negative and Gram-positive bacteria (including methicillin-resistant Staphylococcus aureus) (minimum inhibitory concentrations ≤ 25 μM) and relatively low hemolytic activity against human erythrocytes (LD50 = 100 μM). The peptide therefore represents a candidate for drug development.
Bibliografie:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	1532-0456 1878-1659
DOI:	10.1016/j.cbpc.2005.11.022