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Study on interaction between curcumin and pepsin by spectroscopic and docking methods
- Ying, Ming, Huang, Fengwen, Ye, Haidong, Xu, Hong, Shen, Liangliang, Huan, Tianwen, Huang, Shitong, Xie, Jiangfeng, Tian, Shengli, Hu, Zhangli, He, Zhendan, Lu, Jun, Zhou, Kai
- International journal of biological macromolecules 2015 v.79 pp. 201-208
- absorbance, binding sites, circular dichroism spectroscopy, curcumin, energy transfer, fluorescence, hydrogen bonding, hydrophobicity, molecular models, pH, pepsin, stomach, temperature, thermodynamics, tryptophan, tyrosine, ultraviolet-visible spectroscopy
- The interaction between curcumin and pepsin was investigated by fluorescence, synchronous fluorescence, UV–vis absorption, circular dichroism (CD), and molecular docking. Under physiological pH value in stomach, the fluorescence of pepsin can be quenched effectively by curcumin via a combined quenching process. Binding constant (Ka) and binding site number (n) of curcumin to pepsin were obtained. According to the theory of Förster's non-radiation energy transfer, the distance r between pepsin and curcumin was found to be 2.45nm within the curcumin–pepsin complex, which implies that the energy transfer occurs between curcumin and pepsin, leading to the quenching of pepsin fluorescence. Fluorescence experiments also suggest that curcumin is located more closely to tryptophan residues than tyrosine residues. CD spectra together with UV–vis absorbance studies show that binding of curcumin to pepsin results in the extension of peptide strands of pepsin with loss of some β-sheet structures. Thermodynamic parameters calculated from the binding constants at different temperatures reveal that hydrophobic force plays a major role in stabilizing the curcumin–pepsin complex. In addition, docking results support the above experimental findings and suggest the possible hydrogen bonds of curcumin with Thr-77, Thr-218, and Glu-287 of pepsin, which help further stabilize the curcumin–pepsin complex.