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Chemical biology & drug design 2014-Jul

A lectin from Spatholobus parviflorus inhibits Aspergillus flavus α-amylase: enzyme kinetics and thermodynamic studies.

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Ignatius Tintu
Joseph Abhilash
Kalarickal V Dileep
Anu Augustine
Madathilkovilakath Haridas
Chittalakkottu Sadasivan

Keywords

Abstract

Aspergillus flavus is a commonly found fungal pathogen which produces structurally related and highly toxic secondary metabolites, aflatoxins. It has been proposed that α-amylase inhibitors may limit the ability of the fungus to produce aflatoxins. Hence, this enzyme is a potent target for the development of antifungal agents. In this study, it was found that Spatholobus parviflorus seed lectin (SPL) can inhibit the growth of A. flavus with a MIC value of 1.5 mg/mL. The enzyme kinetics, molecular modeling and isothermal titration calorimetric studies suggest that SPL can inhibit α-amylase with Ki value of 0.0042 mm. Hence, it is suggested that the antifungal activity of SPL might be partly due to its ability to inhibit the enzyme α-amylase.

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