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Title 

Isolation and functional analysis of a 24-residue linear α-helical antimicrobial peptide from Korean blackish cicada, Cryptotympana dubia (Homoptera).

Authors 

Doo Sang ParkJ Y LeemEun Young SuhJ H HurHyun Woo OhHo Yong Park

Publisher 

Wiley-Blackwell

Issue Date 

2007

Citation 

Archives of Insect Biochemistry and Physiology, vol. 66, no. 4, pp. 204-213

Keywords 

amino acid sequenceantimicrobial peptidecryptonincryptotympana dubiaantimicrobial cationic peptidehemolytic agentanimalcell membrane permeabilitycircular dichroismconfocal microscopy

Abstract 

A new antimicrobial peptide, cryptonin, was isolated and characterized from the adult Korean blackish cicada, Cryptotympana dubia. It consists of 24 amino acid residues and has a molecular weight of 2,704 Da on mass spectroscopy. The predicted α-helical structure analysis and increased helix percent in 40% trifloroethanol of cryptonin suggests that it belongs to the typical linear α-helix forming peptide. Binding of the biotin-labeled cryptonin at the surface of E. coli cells and increased influx of propidium iodide in E. coli after cryptonin treatment indicates that it kills microbial cells by binding bacterial cell surfaces and disrupting the cell permeability. Cryptonin showed strong antibacterial (MIC 1.56-25 μg/ml) and antifungal (MIC 3.12-50 μg/ml) activities against tested bacteria and fungi including two antibiotic-resistant bacterial strains; methicilin-resistant S. aureus and vancomycin-resistant Enterococci (MIC 25 μg/ml, each).

ISSN 

0739-4462

Link 

http://dx.doi.org/10.1002/arch.20213

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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