Bioscience, Biotechnology, and Biochemistry
Online ISSN : 1347-6947
Print ISSN : 0916-8451
Microbiology & Fermentation Technology Note
Inhibition of the Bacterial Surface Protein Anchoring Transpeptidase Sortase by Isoquinoline Alkaloids
Soo-Hwan KIMDong-Sun SHINMi-Na OHSoon-Chun CHUNGJang-Suk LEEKi-Bong OH
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JOURNAL FREE ACCESS

2004 Volume 68 Issue 2 Pages 421-424

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Abstract
The inhibitory activity of Coptis chinensis rhizome-derived material was evaluated against sortase, a bacterial surface protein anchoring transpeptidase, from Staphylococcus aureus ATCC 6538p and compared to that of four commercially available isoquinoline alkaloids. The biologically active constituent of C. chinensis extract was characterized as the isoquinoline alkaloid, berberine chloride, by spectral analysis. The isolate was a potent inhibitor of sortase, with an IC50 value of 8.7 μg/ml and had antibacterial activity against Gram-positive bacteria with a minimum inhibitory concentration (MIC) in the range of 50–400 μg/ml. Among the four isoquinoline alkaloids tested, berberine chloride had strong inhibitory activity. These results indicate that berberine is a possible candidate for the development of a bacterial sortase inhibitor.
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© 2004 by Japan Society for Bioscience, Biotechnology, and Agrochemistry
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