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Two novel antimicrobial peptides from skin secretions of the frog, Rana nigrovittata
Author(s) -
Liu Xiuhong,
Liu Rui,
Wei Lin,
Yang Hailong,
Zhang Keyun,
Liu Jingze,
Lai Ren
Publication year - 2011
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.1309
Subject(s) - edman degradation , peptide , genbank , amino acid , complementary dna , antimicrobial peptides , peptide sequence , antimicrobial , biology , biochemistry , cdna library , bacteria , signal peptide , microbiology and biotechnology , gene , genetics
Two novel antimicrobial peptides with similarity to brevinin‐2 family are purified and characterized from the skin secretions of the frog, Rana nigrovittata . Their amino acid sequences were determined as GAFGNFLKGVAKKAGLKILSIAQCKLSGTC ( brevinin‐2‐RN1 ) and GAFGNFLKGVAKKAGLKILSIAQCKLFGTC ( brevinin‐2‐RN2 ), respectively, by Edman degradation. Different from brevinin‐2, which is composed of 33 amino acid residues (aa), both brevinin‐2‐RN1 and ‐RN2 contain 30 aa. Five cDNA sequences (Genbank accession numbers, EU136465‐9) encoding precursors of brevinin‐2‐RN1 and ‐RN2 were screened from the skin cDNA library of R. nigrovittata . These precursors are composed of 72 aa including a predicted signal peptide, an acidic spacer peptide, and a mature brevinin‐2‐RN . Both brevinin‐2‐RN1 and ‐RN2 showed strong antimicrobial activities against gram‐positive and gram‐negative bacteria and fungi. The current work identified and characterized two novel antimicrobial peptides with unique primary structure. Copyright © 2010 European Peptide Society and John Wiley & Sons, Ltd.