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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/56283
Title: Brucyclin, a novel antimicrobial peptide structurally designed from the antibacterial plant peptide, Brucin
Authors: Thakorn Sornwatana
Nuanchawee Wetprasit
Somchoke Traewachiwiphak
Thanawat Phongsak
Sittiruk Roytrakul
Rajabhat University
Ramkhamhaeng University
Mahidol University
Thailand National Center for Genetic Engineering and Biotechnology
Keywords: Medicine;Pharmacology, Toxicology and Pharmaceutics
Issue Date: 1-Feb-2020
Citation: Journal of Applied Pharmaceutical Science. Vol.10, No.2 (2020), 13-20
Abstract: © 2020 Thakorn Sornwatana et al. A novel antimicrobial cyclic peptide, Brucyclin, was rationally designed from the original antibacterial plant peptide, Brucin. The chemically synthesized Brucyclin consists of amino acid sequence; (NH2-Gln-His-Thr-Leu-Cys-Met-Cys-Gly-Gly-Ala-Thr-Trp-COOH), with a molecular mass of m/z 1290. In the antimicrobial assay with 31 strains of pathogenic microorganisms, the peptide exhibited the most antimicrobial activity with a minimum inhibitory concentration (MIC) values ranging from 50 to 100 μg/ml against two strains of Gram-negative bacteria (Vibrio cholera non O1, non O139 and Klebsiella oxytoca), one strain of Gram-positive bacterium (Bacillus subtilis), and one strain of yeast (Candida albicans), respectively. Structural analysis of Brucyclin indicated that it has a neutral charge with a hydrophobicity ratio of 50% and pI value of 6.72, respectively. The results from this study suggested that the Brucyclin is a new antibiotic peptide that might be an alternative potent drug for treatment of various infectious diseases caused by pathogenic microorganisms.
URI: http://repository.li.mahidol.ac.th/dspace/handle/123456789/56283
metadata.dc.identifier.url: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85084076303&origin=inward
ISSN: 22313354
Appears in Collections:Scopus 2020

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