Probing the structural interactions between methotrexate and dexamethasone with muscle cystatin: a biophysical study |
| |
| Authors: | Mohammad Aatif Aaliya Shah Medha Priyadarshini Mohd Farhan |
| |
| Affiliation: | 1. Department of Public Health, College of Applied Medical Sciences, King Faisal University, Al Ahsa, Kingdom Saudi Arabia;2. Department of Biochemistry, SKIMS Medical College, Srinagar, India;3. Department of Medicine, University of Chicago, Chicago, IL, USA;4. Department of Biology, College of Basic Sciences, King Faisal University, Al Ahsa, Kingdom Saudi Arabia |
| |
| Abstract: | AbstractDrug protein interactions have gained considerable attention over the past many years. In the current communication the association of muscle cystatin (MC) with anti-rheumatic drugs methotrexate and dexamethasone was studied by thiol proteinase inhibitor assay, ultra violet (UV) absorption, fluorescence spectroscopy, and fluorescence transform infra-red spectroscopy (FTIR). A static pattern of quenching was noticed between muscle cystatin and methotrexate (MTX). Binding constant (Ka) of methotrexate to muscle cystatin was found to be 1?×?10?7 M?1 and the stoichiometry of binding was calculated to be one. Fluorescence measurement of the emission quenching reveals that the quenching process of cystatin by dexamethasone (DXN) was also static. The stoichiometry of binding and binding constant was also obtained. Additional evidence regarding MTX–MC and DXN–MC was obtained from UV spectroscopy and FTIR spectroscopic results. Such spectroscopic studies would help in modelling new candidate drugs for rheumatoid arthritis based on their cystatin binding profile.Communicated by Ramaswamy H. Sarma |
| |
| Keywords: | Methotrexate dexamethasone ultra-violet muscle cystatin fluorescence transform infra-red spectroscopy cystatin |
|
|
