1. Vulgarinin, a broad-spectrum antifungal peptide from haricot beans (Phaseolus vulgaris)
Jack Ho Wong, Tzi Bun Ng Int J Biochem Cell Biol. 2005 Aug;37(8):1626-32. doi: 10.1016/j.biocel.2005.02.022. Epub 2005 Mar 9.
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.
2. A mitogenic defensin from white cloud beans (Phaseolus vulgaris)
Jack Ho Wong, Xiao Qing Zhang, He Xiang Wang, Tzi Bun Ng Peptides. 2006 Sep;27(9):2075-81. doi: 10.1016/j.peptides.2006.03.020. Epub 2006 May 9.
A peptide, with a molecular mass of 7458 Da, was purified from the seeds of white cloud beans (Phaseolus vulgaris cv. 'white cloud bean'). This peptide was isolated using a simple protocol consisting of affinity chromatography on Affi-gel blue gel and gel filtration on Superdex 75. The peptide had both antifungal and antibacterial activities. It reduced the activity of HIV-1 reverse transcriptase and it also inhibited translation in a cell-free rabbit reticulocyte lysate system. Its antifungal activity was retained after incubation with trypsin but was reduced when the ambient ionic strength was raised. The peptide elicited a mitogenic response from mouse splenocytes but did not stimulate nitric oxide production in mouse macrophages.
3. Limenin, a defensin-like peptide with multiple exploitable activities from shelf beans
Jack H Wong, T B Ng J Pept Sci. 2006 May;12(5):341-6. doi: 10.1002/psc.732.
From the seeds of the shelf bean, an antifungal peptide with a molecular mass of 6.5 kDa was isolated. The isolation procedure comprised affinity chromatography on Affi-gel blue gel, ion exchange chromatography on Mono S, and gel filtration on Superdex 75. The peptide was adsorbed on Affi-gel blue gel and Mono S. It potently suppressed mycelial growth in Botrytis cinerea, Fusarium oxysporum, and Mycosphaerella arachidicola with an IC(50) of 2.9, 2.1, and 0.34 microM, respectively. It exerted antibacterial activity toward several bacterial species with an IC(50) approximating 100 microM. [Methyl-(3)H]-thymidine incorporation into isolated mouse splenocytes was stimulated. [Methyl-(3)H]-thymidine incorporation into M1 (myeloma) and L1210 (leukemia) cells was inhibited. The peptide reduced the activity of HIV-1 reverse transcriptase and also inhibited translation in a cell-free rabbit reticulocyte lysate system.
