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Study on interaction between curcumin and pepsin by spectroscopic and docking methods.

Ming Ying1, Fengwen Huang1, Haidong Ye1

  • 1College of Life Sciences, Shenzhen Key Laboratory of Marine Bioresources and Ecology/Shen Zhen Key Laboratory of Microbial Genetic Engineering, Shenzhen University, Shenzhen 518060, China.

International Journal of Biological Macromolecules
|May 6, 2015
PubMed
Summary
This summary is machine-generated.

Curcumin effectively binds to pepsin, altering its structure and quenching fluorescence through energy transfer. Hydrophobic interactions and hydrogen bonds stabilize this curcumin-pepsin complex, impacting protein structure.

Keywords:
CurcuminInteractionPepsin

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Pharmacology

Background:

  • Pepsin is a key digestive enzyme in the stomach.
  • Curcumin, a compound from turmeric, exhibits various biological activities.
  • Understanding their interaction is crucial for potential therapeutic applications.

Purpose of the Study:

  • To investigate the molecular interaction between curcumin and pepsin.
  • To elucidate the binding mechanism and structural changes induced by curcumin in pepsin.

Main Methods:

  • Fluorescence spectroscopy (fluorescence, synchronous fluorescence)
  • UV-vis absorption spectroscopy
  • Circular dichroism (CD) spectroscopy
  • Förster's non-radiation energy transfer theory
  • Molecular docking

Main Results:

  • Curcumin effectively quenched pepsin fluorescence via a combined quenching process.
  • Binding analysis yielded binding constant (Ka) and binding site number (n).
  • Energy transfer occurred at a distance of 2.45 nm, indicating close proximity.
  • Curcumin binding induced peptide strand extension and loss of β-sheet structures in pepsin.
  • Hydrophobic force was identified as the primary stabilizing force for the complex.
  • Molecular docking suggested hydrogen bonds between curcumin and specific pepsin residues (Thr-77, Thr-218, Glu-287).

Conclusions:

  • Curcumin interacts with pepsin, leading to structural modifications and fluorescence quenching.
  • The interaction is primarily driven by hydrophobic forces and stabilized by hydrogen bonds.
  • This study provides insights into the molecular basis of curcumin-pepsin interaction.