Characterization of intermolecular interaction between cyanidin‐3‐glucoside and bovine serum albumin: Spectroscopic and molecular docking methods |
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| Authors: | Jie‐hua Shi Jing Wang Ying‐yao Zhu Jun Chen |
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| Affiliation: | 1. College of Pharmaceutical Sciences, Zhejiang University of Technology, Hangzhou, China;2. State Key Laboratory Breeding Base of Green Chemistry Synthesis Technology, Zhejiang University of Technology, Hangzhou, China |
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| Abstract: | The intermolecular interaction between cyanidin‐3‐glucoside (Cy‐3‐G) and bovine serum albumin (BSA) was investigated using fluorescence, circular dichroism and molecular docking methods. The experimental results revealed that the fluorescence quenching of BSA at 338 nm by Cy‐3‐G resulted from the formation of Cy‐3‐G–BSA complex. The number of binding sites (n) for Cy‐3‐G binding on BSA was approximately equal to 1. The experimental and molecular docking results revealed that after binding Cy‐3‐G to BSA, Cy‐3‐G is closer to the Tyr residue than the Trp residue, the secondary structure of BSA almost not change, the binding process of Cy‐3‐G with BSA is spontaneous, and Cy‐3‐G can be inserted into the hydrophobic cavity of BSA (site II′) in the binding process of Cy‐3‐G with BSA. Moreover, based on the sign and magnitude of the enthalpy and entropy changes (ΔH0 = – 29.64 kcal/mol and ΔS0 = – 69.51 cal/mol K) and the molecular docking results, it can be suggested that the main interaction forces of Cy‐3‐G with BSA are Van der Waals and hydrogen bonding interactions. Copyright © 2013 John Wiley & Sons, Ltd. |
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| Keywords: | Cyanidin‐3‐glucoside Bovine serum albumin Fluorescence spectroscopy Circular dichroism Molecular docking |
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