HUSCAP logo Hokkaido Univ. logo

Hokkaido University Collection of Scholarly and Academic Papers >
Research Center for Zoonosis Control >
Peer-reviewed Journal Articles, etc >

Functional analysis of an α-helical antimicrobial peptide derived from a novel mouse defensin-like gene

Files in This Item:
BBRC398-4_778-784.pdf1.92 MBPDFView/Open
Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/43910

Title: Functional analysis of an α-helical antimicrobial peptide derived from a novel mouse defensin-like gene
Authors: Kawaguchi, Akira Browse this author
Suzuki, Tadaki Browse this author
Kimura, Takashi Browse this author
Sakai, Naoki Browse this author
Ayabe, Tokiyoshi Browse this author
Sawa, Hirofumi Browse this author
Hasegawa, Hideki Browse this author
Keywords: Antimicrobial peptide
Cationic α-helical peptide
Defensin
Bactericidal activity
CD spectroscopy
Issue Date: 6-Aug-2010
Publisher: Elsevier
Journal Title: Biochemical and Biophysical Research Communications
Volume: 398
Issue: 4
Start Page: 778
End Page: 784
Publisher DOI: 10.1016/j.bbrc.2010.07.028
PMID: 20637182
Abstract: Gene-encoded antimicrobial peptides (AMPs) are an essential component of the innate immune system in many species. Analysis of β-defensin gene expression in mouse tissue using primers that were specific for conserved sequences located outside of the β-defensin translated region identified a novel small gene. The novel gene had an open reading frame of 114 basepairs and encoded a predicted protein of 37 amino acid residues. A search of the genome database revealed that the gene locus and the sequence of exon 1 of this novel gene were similar to subgroup 1 mouse β-defensins. A small peptide, K17 (FSPQMLQDIIEKKTKIL), derived from the amino acid sequence of this novel gene was synthesized. Circular dichroism (CD) spectroscopic analysis of chemically synthesized peptide demonstrated that the peptide exhibited random coil conformation in aqueous solution, but the peptide adopted helical conformation in the presence of trifluoroethanol or sodium dodecyl sulfate, a membrane mimicking environment. The peptide exhibited bactericidal activity against Salmonella enterica serovar Typhimurium (Gram negative) and Staphylococcus aureus (Gram positive); it was not cytotoxic in cultures of mammalian cells or hemolytic in cultures of erythrocytes. These results suggested that K17 may be a candidate therapeutic for the treatment of bacterial infection.
Type: article (author version)
URI: http://hdl.handle.net/2115/43910
Appears in Collections:人獣共通感染症リサーチセンター (Research Center for Zoonosis Control) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 川口 晶

Export metadata:

OAI-PMH ( junii2 , jpcoar )

MathJax is now OFF:


 

 - Hokkaido University