Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10836173 | Peptides | 2005 | 7 Pages |
Abstract
An antifungal peptide with a molecular mass around 7Â kDa and an N-terminal sequence highly homologous to defensin was isolated from ground beans (Vigna sesquipedalis cv. 'Ground Bean'). The peptide was adsorbed on Affi-gel blue gel and on Mono S. It exerted an antifungal action on Botrytis cinerea, Fusarium oxysporum and Mycosphaerella arachidicola; and an antibacterial action on Escherichia coli B, Proteus vulgaris, Mycobacterium phlei and Bacillus megaterium. The antimicrobial activity was inhibited in presence of the 5Â mM CaCl2 and MgCl2, but no inhibition was observed in 5Â mM NaCl. The peptide exerted antiproliferative activity toward breast cancer (MCF-7) cells and leukemia M1 cells, this activity could not be inhibited by the ions mentioned above. It also exhibited some inhibitory activity toward human immunodeficiency virus-type 1 reverse transcriptase.
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Authors
Jack Ho Wong, Tzi Bun Ng,