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Purification of Angularin, A Novel Antifungal Peptide from Adzuki Beans

✍ Scribed by Dr X. Y. Ye; T. B. Ng

Publisher
John Wiley and Sons
Year
2002
Tongue
English
Weight
122 KB
Volume
8
Category
Article
ISSN
1075-2617

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✦ Synopsis

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 IC~50~ of 14.3 µM. Fusarium oxysporum and Rhizoctonia solani were not inhibited. Angularin demonstrated inhibitory activity on translation in the rabbit reticulocyte lysate system (IC~50~ = 8.0 µM) 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. Copyright © 2002 European Peptide Society and John Wiley & Sons, Ltd.

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