Open Access Peer-reviewed Research Article

Binding studies of trans-resveratrol with superoxide dismutase (SOD1): Docking assessment and Thermoanalysis

Main Article Content

Janhvi Dureja
Renu Chadha corresponding author
Maninder Karan
Akshita Jindal
Kunal Chadha


The binding pursuits of trans-resveratrol (t-RSV), an amazing health supplement are investigated with an antioxidant enzyme, superoxide dismutase (SOD1). The aim of the study is to dock t-RSV on the adrenaline binding site on SOD1 in order to explore its potential to act as a safety net against amyotrophic lateral sclerosis (ALS), a fatal neurodegenerative disorder that affects motor neurons. In silico GLIDE docking methodology and in vitro microcalorimetry technique is utilized for the investigation of binding parameters of t-RSV with SOD1. The study provides useful and distinct information about the amino acids involved in the interactions at molecular level along with the nature of forces involved in binding of t-RSV with SOD1.  The docking analysis using the scoring functions of Schrodinger's Glide package depicts that GLU100, PRO28, LYS23, TRP32 residues of the peptide backbone on SOD 1 interact with phenolic groups of t-RSV. The information on thermodynamic parameters, i.e. binding constant (Kb), free energy (ΔG) and enthalpy (ΔH) generated through calorimetric titrations suggests that the reaction between t-RSV and SOD 1 is spontaneous and exothermic. Both the studies are found to be in close agreement with each other based as far as the magnitude of binding constant (Kb =9.9 x10 4) is concerned.

trans-Resveratrol, superoxide dismutase, docking, microcalorimetry, binding constant, free energy

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How to Cite
Dureja, J., Chadha, R., Karan, M., Jindal, A., & Chadha, K. (2019). Binding studies of trans-resveratrol with superoxide dismutase (SOD1): Docking assessment and Thermoanalysis. Journal of Pharmaceutical and Biopharmaceutical Research, 1(1), 21-27.


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