Journal
PEPTIDES
Volume 24, Issue 7, Pages 963-968Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/S0196-9781(03)00192-X
Keywords
antifungal peptides; isolation; bean; Gymnocladus chinensis
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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 muM for the former fungus and 10 muM 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 muM. (C) 2003 Elsevier Inc. All rights reserved.
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