Journal
MOLECULAR PHARMACEUTICS
Volume 14, Issue 5, Pages 1656-1665Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.molpharmaceut.6b01124
Keywords
circular dichroism; differential scanning calorimetry; eperisone hydrochloride; esterase-like activity; human serum albumin; isothermal titration calorimetry; molecular docking; muscle relaxant
Funding
- Yeungnam University, Republic of Korea
- Ministry of Education, Science and Technology (MEST), Republic of Korea [K16281]
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Eperisone hydrochloride (EH) is widely used as a muscle relaxant for patients with muscular contracture, low back pain, or spasticity. Human serum albumin (HSA) is a highly soluble negatively charged, endogenous and abundant plasma protein ascribed with the ligand binding and transport properties. The current study was undertaken to explore the interaction between EH and the serum transport protein, HSA. Study of the interaction between HSA and EH was carried by UV-vis, fluorescence quenching, circular dichroism (CD), Fourier transform infrared (FTIR) spectroscopy, Forster's resonance energy transfer, isothermal titration calorimetry and differential scanning calorimetry. Tryptophan fluorescence intensity of HSA was strongly quenched by EH. The binding constants (K-b) were obtained by fluorescence quenching, and results show that the HSA-EH interaction revealed a static mode of quenching with binding constant K-b approximate to 10(4) reflecting high affinity of EH for HSA. The negative Delta G degrees value for binding indicated that HSA-Eli interaction was a spontaneous process. Thermodynamic analysis shows HSA-EH complex formation occurs primarily due to hydrophobic interactions, and hydrogen bonds were facilitated at the binding of EH. EH binding induces alpha-helix of HSA as obtained by far-UV CD and FTIR spectroscopy. In addition, the distance between EH (acceptor) and Trp residue of HSA (donor) was calculated 118 nm using Forster's resonance energy transfer theory. Furthermore, molecular docking results revealed EH binds with HSA, and binding site was positioned in Sudlow Site I of HSA (subdomain IIA). This work provides a useful experimental strategy for studying the interaction of myorelaxant with HSA, helping to understand the activity and mechanism of drug binding.
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