Publication: Brucyclin, a novel antimicrobial peptide structurally designed from the antibacterial plant peptide, Brucin
Issued Date
2020-02-01
Resource Type
ISSN
22313354
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2-s2.0-85084076303
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Mahidol University
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SCOPUS
Bibliographic Citation
Journal of Applied Pharmaceutical Science. Vol.10, No.2 (2020), 13-20
Suggested Citation
Thakorn Sornwatana, Nuanchawee Wetprasit, Somchoke Traewachiwiphak, Thanawat Phongsak, Sittiruk Roytrakul Brucyclin, a novel antimicrobial peptide structurally designed from the antibacterial plant peptide, Brucin. Journal of Applied Pharmaceutical Science. Vol.10, No.2 (2020), 13-20. doi:10.7324/JAPS.2020.102003 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/56283
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Title
Brucyclin, a novel antimicrobial peptide structurally designed from the antibacterial plant peptide, Brucin
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.