Abstract
From the seeds of haricot beans ( Phaseolus vulgaris), an antifungal peptide with a molecular mass around 7 kDa was purified by using a simple protocol consisting of affinity chromatography on Affi-gel blue gel and gel filtration on Superdex 75. This peptide named vulgarinin manifested an antifungal activity toward fungal species such as Fusarium oxysporum, Mycosphaerella arachidicola, Physalospora piricola and Botrytis cinerea, and an antibacterial action on Mycobacterium phlei, Bacillus megaterium, Bacillus subtilis and Proteus vulgaris. It also inhibited proliferation in leukemia cell lines L1210 and M1 and breast cancer cell line MCF-7. This peptide could reduce the activity of HIV-1 reverse transcriptase and inhibited translation in a cell-free rabbit reticulocyte lysate system. Its antifungal activity was retained after incubation with trypsin.
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