Antimicrobial, α-Glucosidase and Alkaline Phosphatase Inhibitory Activities of Bergenin, The Major Constituent of Cissus populnea Roots

Abstract

Bergenin (1) was isolated as the major compound of the Roots of Cissus populnea. Its structure was elucidated on the basis of spectral analysis, including 1D and 2D NMR experiments and Mass Spectrometry (MS) as well as by comparison with available data in the literature. Bergenin (1) was evaluated for its antimicrobial activity against four bacteria strains (Salmonella typhi ATCC6539, Salmonella typhi (isolate), Pseudomonas aeruginosa ATCC9721 and Escherichia coli (isolate)) and four yeasts (Candida albicans ATCC9002, Candida parapsilosis ATCC22019, Candida krusei (isolate) and Candida albicans (isolate)) using micro broth dilution method and for its enzymatic activities against α-glucosidase and Alkaline Phosphatase (h-TNAP and h-IAP). It exhibited significant to moderate antibacterial activities with the MIC ranking from 8 to 64 μg.mL-1, while it appeared to be inactive (MIC>125 μg.mL-1) against all the tested yeast. However, it was found to be high potent inhibitor of both h-TNAP and h-IAP alkaline phosphatase isoenzymes, with a selectivity for the h-TNAP. Daucosterol (4) and a mixture of sitosterol (2+3) were also obtained and were screening for the same bioactivities.