A Lectin from Spatholobus parviflorus Inhibits Aspergillus flavus α-Amylase: Enzyme Kinetics and Thermodynamic Studies

• Published in: Chemical biology & drug design 2014-07, Vol.84 (1), p.116-122
• Main Authors: Tintu, Ignatius, Abhilash, Joseph, Dileep, Kalarickal V., Augustine, Anu, Haridas, Madathilkovilakath, Sadasivan, Chittalakkottu
• Format: Article
• Language: English
• Subjects: alpha-Amylases - antagonists & inhibitors; alpha-Amylases - chemistry; alpha-Amylases - metabolism; Antifungal Agents - chemistry; Antifungal Agents - isolation & purification; Antifungal Agents - pharmacology; Aspergillosis - drug therapy; Aspergillus flavus; Aspergillus flavus - drug effects; Aspergillus flavus - enzymology; enzyme kinetics; Fabaceae - chemistry; Humans; Kinetics; lectin; Molecular Docking Simulation; Plant Lectins - chemistry; Plant Lectins - isolation & purification; Plant Lectins - pharmacology; Thermodynamics; α-amylase
• ISSN: 1747-0277; 1747-0285
• DOI: 10.1111/cbdd.12291

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. It has been proposed that α‐amylase inhibitors may limit the ability of the fungus to produce aflatoxins. α‐amylase is a potent target for the development of anti‐fungal agents. Spatholobus parviflorus seed lectin (SPL) can inhibit the growth of A flavus with a MIC value of 1.5 mg/mL.