Authors: Li, Miao; Wang, Hexiang; Bun Ng, Tzi

Source: Protein and Peptide Letters, Volume 18, Number 6, June 2011 , pp. 594-600(7)

Publisher: Bentham Science Publishers

Abstract:

A 7.3-kDa antifungal peptide was purified from dried red kidney beans. The purification procedure entailed ion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, ion exchange chromatography on CM-cellulose, followed by fast protein liquid chromatography-gel filtration on Superdex 75. The peptide was unadsorbed on DEAE-cellulose but adsorbed on Affi-gel blue gel and CM-cellulose. It exhibited a molecular mass of 7.3 kDa in gel filtration and also in SDS-polyacrylamide gel electrophoresis, indicating that it is a single-chained protein. The N-terminal sequence of the peptide was DGVCFGGLANGDRT. The peptide exerted an antifungal action on Fusarium oxysporum with an IC50 of 3.8±0.4 μM (mean±SD, n=3). It also inhibited mycelial growth in Mycosphaerella arachidicola. It suppressed growth of lymphoma MBL2 cells and leukemia L1210 cells with an IC50 of 5.2±0.4 μM and 7.6±0.6 μM, respectively. HIV-1 reverse transcriptase was inhibited with an IC50 of 40±3.2 μM. However, no activity was demonstrated toward other viral enzymes.

Keywords: Purification; characterization; antifungal; antiproliferative; HIV-1; leguminous seeds

Document Type: Research article

DOI: http://dx.doi.org/10.2174/092986611795222803

Publication date: 2011-06-01

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• Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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