| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1185755 | Food Chemistry | 2012 | 7 Pages |
A 5447 Da antifungal peptide with an N-terminal sequence highly homologous to plant defensins was purified from Phaseolus vulgaris cv. ‘King Pole Bean’ by anion-exchange chromatography on Q Sepharose and FPLC-gel filtration on Superdex 75. The isolated peptide inhibited growth of a number of fungal species, including Mycosphaerella arachidicola, Saccharomyces cerevisiae and Candida albicans, with IC50 values of 3.9, 4.0 and 8.4 μM, respectively. Using the membrane non-permeable DNA-binding dye SYTOX green, it was found that the peptide increased the cell membrane permeability of M. arachidicola, S. cerevisiae and C. albicans.
► A peptide resembling plant defensins in sequence was purified from King Pole Bean. ► The peptide permeabilizes yeast cell membrane as revealed by SYTOX green staining. ► The antifungal peptide induces gene expression of tumour necrosis factor – α.
