title: Binding of anti-cardiovascular drug to serum albumin: an insight in the light of spectroscopic and computational approaches.
abstract: Isoprenaline hydrochloride is a potential cardiovascular drug helps in the smooth functioning of the heart muscles. So, we have performed the binding study of ISO with BSA. This study was investigated by UV absorption, fluorescence, synchronous fluorescence, circular dichroism, etc. The analysis of intrinsic fluorescence data showed the low binding affinity of ISO. The binding constant Kbwas 2.8 × 103 M-1 and binding stoichiometry (n) was approximately one and the Gibb's free energy change at 310 K was determined to be -8.69 kcal mol-1. Negative Gibb's free energy change shows the spontaneity of the BSA and ISO interaction. We have found ISO-induced alternation in the UV absorption, synchronous fluorescence and CD spectra in the absence and presence of the quencher indicates the complex formation. In synchronous fluorescence, red shift was obtained because of the complex formation of BSA and ISO. The distance (r) between the BSA (donor) and ISO (acceptor) was 2.89 nm, determined by FRET. DLS measurements interpreted complex formation due to the reduction in hydrodynamic radii of the protein in the presence of the drug. The binding site of ISO was found to be nearer to Trp 134 with the help of molecular docking and the ΔG° was found to be -10.2 kcal mol-1. The esterase activity result suggests that ISO acts as competitive inhibitor. Thus, this study would help to determine the binding capacity of the drug to the protein which may indicate the efficiency of diffusion of ISO into the blood for the treatment of heart diseases.
authors.affiliation: a Interdisciplinary Biotechnology Unit , Aligarh Muslim University , Aligarh , India.
authors.forename: Tajalli Ilm
authors.initials: TI
authors.lastname: Chandel
authors.affiliation: b School of Medical Biotechnology , YeungNam University , Gyeongsan , Republic of Korea.
authors.forename: Gulam
authors.initials: G
authors.lastname: Rabbani
authors.affiliation: a Interdisciplinary Biotechnology Unit , Aligarh Muslim University , Aligarh , India.
authors.forename: MohsinVahid
authors.initials: M
authors.lastname: Khan
authors.affiliation: a Interdisciplinary Biotechnology Unit , Aligarh Muslim University , Aligarh , India.
authors.forename: Masihuz
authors.initials: M
authors.lastname: Zaman
authors.affiliation: a Interdisciplinary Biotechnology Unit , Aligarh Muslim University , Aligarh , India.
authors.forename: Parvez
authors.initials: P
authors.lastname: Alam
authors.affiliation: c Molecular Biology Department, Genetic Engineering Division , National Research Centre , Cairo , Egypt.
authors.forename: Yasser
authors.initials: Y
authors.lastname: E Shahein
authors.affiliation: a Interdisciplinary Biotechnology Unit , Aligarh Muslim University , Aligarh , India.
authors.forename: Rizwan
authors.initials: R
authors.lastname: Hasan Khan
mesh_terms: D000465:Algorithms; D000818:Animals; D001665:Binding Sites; D002316:Cardiotonic Agents / Q000737:chemistry / Q000378:metabolism; D002417:Cattle; D002942:Circular Dichroism / Q000379:methods*; D000067493:Dynamic Light Scattering; D007545:Isoproterenol / Q000737:chemistry* / Q000378:metabolism; D007700:Kinetics; D062105:Molecular Docking Simulation; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000737:chemistry* / Q000378:metabolism; D013053:Spectrophotometry / Q000379:methods*; D013816:Thermodynamics
chemical_list: D002316:Cardiotonic Agents; D012710:Serum Albumin, Bovine; D007545:Isoproterenol
keywords: bovine serum albumin; circular dichroism; fluorescence quenching; isoprenaline hydrochloride; synchronous fluorescence