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Spectroscopy and Molecular Modeling Study on the Interaction Between Mycophenolate Mofetil and Pepsin
Xiaoli Ma1, Liuqi Guo1, Qing Wang1
1College of Chemical Engineering, Sichuan University, Chengdu, Sichuan, 610065, China.
Journal of Fluorescence
|December 17, 2015
Summary
Mycophenolate mofetil (MMF) interacts with pepsin, potentially affecting drug distribution. This study used spectroscopy and simulations to reveal binding forces and structural changes.
Area of Science:
- Biochemistry
- Pharmacology
- Molecular Biology
Background:
- Mycophenolate mofetil (MMF) is an immunosuppressant crucial for preventing organ transplant rejection.
- MMF is metabolized to mycophenolic acid, its active form, in the body.
- The interaction between MMF and pepsin in the gastrointestinal tract may influence MMF's absorption and distribution.
Purpose of the Study:
- To investigate the interaction between Mycophenolate mofetil (MMF) and pepsin.
- To elucidate the binding forces and conformational changes induced by this interaction.
- To determine the molecular interaction mechanisms using spectroscopic and computational methods.
Main Methods:
- Fluorescence spectroscopy (three-dimensional and synchronous) to analyze MMF-pepsin binding.
- Förster non-radiative energy transfer (FRET) to calculate interaction distance and efficiency.
- Molecular docking simulations to visualize binding sites and interactions.
Main Results:
- MMF strongly quenched pepsin's fluorescence, indicating binding.
- Hydrophobic forces were identified as the primary binding force.
- MMF binding induced conformational and microenvironment changes in pepsin.
- Docking revealed MMF binding within pepsin's hydrophobic cavity, forming a hydrogen bond with tyrosine 189.
Conclusions:
- MMF binds to pepsin through hydrophobic interactions and hydrogen bonding.
- This interaction causes significant conformational changes in pepsin.
- Understanding this interaction is vital for optimizing MMF therapy and predicting its pharmacokinetics.
