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

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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).
Author(s)
Doo Sang Park; J Y Leem; Eun Young Suh; J H Hur; Hyun Woo OhHo Yong Park
Bibliographic Citation
Archives of Insect Biochemistry and Physiology, vol. 66, no. 4, pp. 204-213
Publication Year
2007
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).
Keyword
Amino acid sequenceAntimicrobial peptideCryptoninCryptotympana dubia
ISSN
0739-4462
Publisher
Wiley
DOI
http://dx.doi.org/10.1002/arch.20213
Type
Article
Appears in Collections:
Jeonbuk Branch Institute > Biological Resource Center > 1. Journal Articles
Division of Bio Technology Innovation > Core Research Facility & Analysis Center > 1. Journal Articles
Division of Biomedical Research > Microbiome Convergence Research Center > 1. Journal Articles
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