Molecular modeling and multispectroscopic studies of the interaction of mesalamine with bovine serum albumin.
The interaction of mesalamine (5-aminosalicylic acid (5-ASA)) with bovine serum albumin (BSA) was investigated by fluorescence quenching, absorption spectroscopy, circular dichroism (CD) techniques, and molecular docking. Thermodynamic parameters (ΔH<0 and ΔS 0) indicated that the hydrogen bond and electrostatic forces played the major role in the binding of 5-ASA to BSA. The results of CD and UV-vis spectroscopy showed that the binding of this drug to BSA induces some conformational changes in BSA. Displacement experiments predicted that the binding of 5-ASA to BSA is located within domain III, Sudlows site 2, that these observations were substantiated by molecular docking studies. In addition, the docking result shows that the 5-ASA in its anionic form mainly interacts with Gln-416 residue through one hydrogen bond between H atom of 5-ASA anion and the adjacent O atom of the hydroxyl group of Gln-416.
Department of Chemistry, Faculty of Science, Razi University, Kermanshah, Iran. Electronic address: nahidshahabadi@yahoo.com.
Nahid
N
Shahabadi
Soraya Moradi
SM
Fili
D000818:Animals; D000894:Anti-Inflammatory Agents, Non-Steroidal / Q000378:metabolism*; D001665:Binding Sites; D002417:Cattle; D002942:Circular Dichroism; D019804:Mesalamine / Q000378:metabolism*; D062105:Molecular Docking Simulation; D011485:Protein Binding; D011487:Protein Conformation / Q000187:drug effects; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet
D000894:Anti-Inflammatory Agents, Non-Steroidal; D012710:Serum Albumin, Bovine; D019804:Mesalamine
BSA; Mesalamine; Molecular docking