Abstract
An antifungal peptide was isolated from the adzuki bean with a procedure involving affinity chromatography on Affi-gel blue gel and ion exchange chromatography on CM-Sepharose. The protein designated angularin was adsorbed on both types of chromatographic media and possessed a molecular weight of 8 kDa. Angularin exhibited antifungal activity against a variety of fungal species including Mycospharella arachidiocola and Botrytis cinerea. It inhibited mycelial growth in B. cinerea with an IC50 of 14.3 microM. Fusarium oxysporum and Rhizoctonia solani were not inhibited. Angularin demonstrated inhibitory activity on translation in the rabbit reticulocyte lysate system (IC50 = 8.0 microM) but did not affect proliferation of splenocytes. The activity of HIV-1 reverse transcriptase was inhibited in the presence of angularin. Its N-terminal sequence was GEPGQKE.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Anti-Bacterial Agents / isolation & purification
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Anti-Bacterial Agents / pharmacology*
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Antifungal Agents / isolation & purification
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Antifungal Agents / pharmacology*
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Chromatography
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Chromatography, Ion Exchange
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Fungi / metabolism
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Fusarium / metabolism
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HIV Reverse Transcriptase / metabolism
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Inhibitory Concentration 50
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Mice
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Mice, Inbred C57BL
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Peptides*
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Plant Proteins / isolation & purification
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Plant Proteins / pharmacology*
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Protein Biosynthesis / drug effects
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Protein Structure, Tertiary
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Rabbits
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Reticulocytes / metabolism
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Reverse Transcriptase Inhibitors / isolation & purification
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Reverse Transcriptase Inhibitors / pharmacology
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Rhizoctonia / metabolism
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Spleen / cytology
Substances
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Anti-Bacterial Agents
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Antifungal Agents
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Peptides
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Plant Proteins
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Reverse Transcriptase Inhibitors
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HIV Reverse Transcriptase