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 seedsPurification, characterization, antifungal, antiproliferative, HIV-1, leguminous seeds
Protein & Peptide Letters
Title: An Antifungal Peptide with Antiproliferative Activity Toward Tumor Cells from Red Kidney Beans
Volume: 18 Issue: 6
Author(s): Miao Li, Hexiang Wang and Tzi Bun Ng
Affiliation:
Keywords: Purification, characterization, antifungal, antiproliferative, HIV-1, leguminous seedsPurification, characterization, antifungal, antiproliferative, HIV-1, leguminous seeds
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.
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Cite this article as:
Li Miao, Wang Hexiang and Bun Ng Tzi, An Antifungal Peptide with Antiproliferative Activity Toward Tumor Cells from Red Kidney Beans, Protein & Peptide Letters 2011; 18 (6) . https://dx.doi.org/10.2174/092986611795222803
DOI https://dx.doi.org/10.2174/092986611795222803 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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