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Interaction Behavior Between Niclosamide and Pepsin Determined by Spectroscopic and Docking Methods.

Liuqi Guo1, Xiaoli Ma1, Jin Yan1

  • 1College of Chemical Engineering, Sichuan University, Chengdu, Sichuan, 610065, People's Republic of China.

Journal of Fluorescence
|September 28, 2015
PubMed
Summary

Niclosamide (NIC) binds to pepsin, altering its structure and inhibiting its activity. This study reveals molecular details of the niclosamide-pepsin interaction, important for understanding drug effects.

Keywords:
BindingFluorescence spectroscopyMolecular modelingNiclosamidePepsin

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Pharmacology

Background:

  • Pepsin is a key digestive enzyme whose function can be modulated by small molecules.
  • Understanding drug-target interactions at a molecular level is crucial for drug development and predicting efficacy.
  • Niclosamide (NIC) is an anthelmintic drug with potential antiviral and anticancer properties, suggesting broader biological activities.

Purpose of the Study:

  • To investigate the molecular interaction mechanism between niclosamide (NIC) and pepsin.
  • To determine the thermodynamic parameters and binding characteristics of NIC-pepsin complex formation.
  • To elucidate how NIC binding affects pepsin's structure, conformation, and enzymatic activity.

Main Methods:

  • Multispectroscopic techniques including fluorescence quenching, synchronous, and 3D fluorescence spectroscopy.
  • Molecular docking simulations to predict binding modes and interactions.
  • In vitro enzyme activity assays to assess the effect of NIC on pepsin's catalytic function.

Main Results:

  • Spectroscopic data revealed changes in pepsin's microenvironment and conformation upon NIC binding.
  • Förster nonradiative energy transfer analysis provided insights into the molecular interaction distance and energy transfer efficiency.
  • NIC binding was found to inhibit pepsin activity in vitro, primarily through hydrophobic interactions and hydrogen bonds at a single site.

Conclusions:

  • Niclosamide (NIC) interacts with pepsin, leading to significant structural and conformational changes.
  • The binding is characterized by hydrophobic interactions and hydrogen bonds, occurring at a single binding site.
  • This study provides molecular-level evidence for NIC's ability to modulate pepsin structure and function.