Insight to nano-curcumin interaction with alpha crystallin: spectroscopy and molecular docking study

Introduction: Alpha Crystallin is a major lens protein, comprising up to 40% of total lens proteins, where its structural function is to assist in maintaining the proper refractive index in the lens. Curcumin was identified as the principle biologically therapeutic compound of turmeric and was found to possess a wide range of beneficial pharmacological properties including anti-inflammatory, anti-oxidant, anti-microbial and anti-cancer activities. In this study we reveal the nano curcumin treatments features upon interaction with alpha crystallin the by using the biophysical method and molecular docking. Materials and methods: The measurement of fluorescence signals provides a sensitive method for monitoring the biochemical environment of a fluorophore and can give us important information about the molecular level of binding of small molecular substances to the protein, such as the binding mechanism, binding constants, and intermolecular distances.Synchronous fluorescence spectra provide information about changes in the molecular microenvironment in the vicinity of functional fluorophores and are used to investigate the conformational changes of proteins. Molecular docking was used to predict the binding site of nano curcumin to the protein by MOE 2015 software. Results and conclusion: Decreasing in the fluorescence intensity upon increasing the concentration of nano curcumin proved that the interaction happened and complex forming. Synchronous spectra showed that the microenvironment of the TRP and TRY for the protein has changed which induced complex forming. Molecular docking indicated that the 28VAL, 45GLN and 22SER were the most sensitive residue in this interaction Conclusion: In this manuscript we determined the binding mechanism and binding behavior of nano curcumin with the alpha crystallin through biophysical and molecular modeling methods.