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A relatively stable antifungal peptide from buckwheat seeds with antiproliferative activity toward cancer cells
Author(s) -
Leung Edwin H. W.,
Ng T. B.
Publication year - 2007
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.891
Subject(s) - peptide , sepharose , chemistry , fusarium oxysporum , molecular mass , biochemistry , cancer cell , splenocyte , size exclusion chromatography , microbiology and biotechnology , biology , in vitro , cancer , enzyme , botany , genetics
An antifungal peptide with a molecular mass of approximately 4 kDa was isolated from buckwheat seeds by using ion‐exchange chromatography on SP‐Sepharose and Q‐Sepharose, and gel filtration on Superdex peptide. The peptide was adsorbed on SP‐Sepharose in 10 m M NH 4 OAc buffer (pH 4.5) and on Q‐Sepharose in 10 m M NH 4 HCO 3 buffer (pH 9.4), and appeared to be highly purified after these two steps. It inhibited mycelial growth in Fusarium oxysporum and Mycosphaerella arachidicola with an IC 50 of 35 and 40 µ M , respectively. Its antifungal activity was stable between 0 and 70 °C, and between pH 1.0/2.0 and 13. It inhibited proliferation of Hep G2 (hepatoma) cells, L1210 (leukemia) cells, breast cancer (MCF‐7) cells, and liver embryonic WRL 68 cells with an IC 50 of 33, 4, 25, and 37 µ M , respectively. On the other hand, the peptide was unable to evoke a mitogenic response from splenocytes or induce nitric oxide production by macrophages. It inhibited HIV‐1 reverse transcriptase with an IC 50 of 5.5 µ M . Copyright © 2007 European Peptide Society and John Wiley & Sons, Ltd.