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Nonylphenol and bisphenol A binding studies with antioxidant enzymes through homology modeling and molecular docking methods

M. Jayakanthan1#, R. Jubendradass2, Shereen Cynthia D’Cruz2, P. P. Mathur1,2,3*

1 Centre for Bioinformatics, School of Life Sciences, Pondicherry University, Pondicherry- 605 014, India
2 Department of Biochemistry and Molecular Biology, School of Life Sciences, Pondicherry University, Pondicherry - 605 014, India
3 KIIT University, Bhubaneswar - 751024, India

#Current address:
CSIR-Centre for Cellular and Molecular Biology, Uppal Road, Hyderabad - 500 007, Andhra Pradesh, India

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Key words: Nonylphenol; Bisphenol A; antioxidant; homology modeling; molecular docking

Abstract
Bisphenol A (BPA) and nonylphenol (NP) are phenolic compounds used widely by the industries. BPA and NP are endocrine disruptors possessing estrogenic properties. Several studies have reported that BPA and NP induce oxidative stress in various organs or cell types in animals, by inhibiting the activities of antioxidant enzymes like catalase, superoxide dismutase, glutathione peroxidase and glutathione reductase. However, it is not understood how BPA and NP interact with these enzymes and inhibit their functions. Hence, it would be significant to check, whether binding sites are available for NP and BPA in antioxidant enzymes. In the present study three-dimensional structures of antioxidant enzymes, catalase, superoxide dismutase, glutathione peroxidase and glutathione reductase were modeled and docked with BPA and NP. Molecular docking studies revealed that BPA and NP have binding pockets in the antioxidant enzymes. Among the antioxidant enzymes, Catalase was maximally inhibited by BPA and superoxide was maximally inhibited by NP.

1. Introduction Molecular docking is an automated

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