Premium
Elucidating the interaction of clofazimine with bovine liver catalase; a comprehensive spectroscopic and molecular docking approach
Author(s) -
Zaman Masihuz,
Nusrat Saima,
Zakariya Syed Mohammad,
Khan Mohsin Vahid,
Ajmal Mohammad Rehan,
Khan Rizwan Hasan
Publication year - 2017
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.2619
Subject(s) - circular dichroism , clofazimine , chemistry , docking (animal) , fluorescence spectroscopy , binding constant , fluorescence , biophysics , crystallography , binding site , biochemistry , biology , medicine , leprosy , physics , nursing , quantum mechanics , immunology
Nowadays, understanding of interface between protein and drugs has become an active research area of interest. These types of interactions provide structural guidelines in drug design with greater clinical efficacy. Thus, structural changes in catalase induced by clofazimine were monitored by various biophysical techniques including UV‐visible spectrometer, fluorescence spectroscopy, circular dichroism, and dynamic light scattering techniques. Increase in absorption spectra (UV‐visible spectrum) confers the complex formation between drug and protein. Fluorescence quenching with a binding constants of 2.47 × 10 4 M −1 revealed that clofazimine binds with protein. Using fluorescence resonance energy transfer, the distance ( r ) between the protein (donor) and drug (acceptor) was found to be 2.89 nm. Negative Gibbs free energy change (Δ G °) revealed that binding process is spontaneous. In addition, an increase in α‐helicity was observed by far‐UV circular dichroism spectra by adding clofazimine to protein. Dynamic light scattering results indicate that topology of bovine liver catalase was slightly altered in the presence of clofazimine. Hydrophobic interactions are the main forces between clofazimine and catalase interaction as depicted by molecular docking studies. Apart from hydrophobic interactions, some hydrogen bonding was also observed during docking method. The results obtained from the present study may establish abundant in optimizing the properties of ligand‐protein mixtures relevant for numerous formulations.