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. 2007 Aug 29;13(10):642–648. doi: 10.1002/psc.893

Lipid transfer proteins from Brassica campestris and mung bean surpass mung bean chitinase in exploitability

Peng Lin 1,†, Lixin Xia 2,†, Jack H Wong 1, T B Ng 1,✉, Xiuyun Ye 3, Shaoyun Wang 3, Shi Xiangzhu 3
PMCID: PMC7167883  PMID: 17726719

Abstract

Antifungal peptides with a molecular mass of 9 kDa and an N‐terminal sequence demonstrating remarkable similarity to those of nonspecific lipid transfer proteins (nsLTPs) were isolated from seeds of the vegetable Brassica campestris and the mung bean. The purified peptides exerted an inhibitory action on mycelial growth in various fungal species. The antifungal activity of Brassica and mung bean nsLTPs were thermostable, pH‐stable, and stable after treatment with pepsin and trypsin. In contrast, the antifungal activity of mung bean chitinase was much less stable to changes in pH and temperature. Brassica LTP inhibited proliferation of hepatoma Hep G2 cells and breast cancer MCF 7 cells with an IC50 of 5.8 and 1.6 µm, respectively, and the activity of HIV‐1 reverse transcriptase with an IC50 of 4 µm. However, mung bean LTP and chitinase were devoid of antiproliferative and HIV‐1 reverse transcriptase inhibitory activities. In contrast to the mung bean LTP, which exhibited antibacterial activity, Brassica LTP was inactive. All three antifungal peptides lacked mitogenic activity toward splenocytes. These results indicate that the two LTPs have more desirable activities than the chitinase and that there is a dissociation between the antifungal and other activities of these antifungal proteins. Copyright © 2007 European Peptide Society and John Wiley & Sons, Ltd.

Keywords: lipid transfer proteins, antifungal proteins, mung bean, Brassica compestris

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