Author(s): Wong JH, Ng TB
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Abstract From the seeds of the Yunnan bean, we purified an antifungal peptide using affinity chromatography on Affi-gel blue gel, FPLC-ion exchange chromatography on Mono S, and FPLC-gel filtration on Superdex 75. The antifungal peptide was adsorbed on Affi-gel blue gel at pH 7.8 and Mono S at pH 4.5. It exhibited a molecular mass of 6.5 kDa in both gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Its N-terminal sequence closely resembled defensin-related peptides. The peptide exerted antifungal activity toward the fungal species Fusarium oxysporum and Mycosphaerella arachidicola, with an IC50 of 2 microM for the former fungus and 10 microM for the latter. It manifested a weaker mitogenic activity toward murine splenocytes than Concanavalin A. It also displayed antiproliferative activity on a murine leukemia (L1210), a hepatoma (HepG2), and a murine leukemia (M1) cell line. It inhibited human immunodeficiency virus-1 reverse transcriptase with an IC50 of 200 microM.
This article was published in Peptides
and referenced in Medicinal & Aromatic Plants