title: Interaction of amphiphilic drugs with human and bovine serum albumins.
abstract: To know the interaction of amphiphilic drugs nortriptyline hydrochloride (NOT) and promazine hydrochloride (PMZ) with serum albumins (i.e., human serum albumin (HSA) and bovine serum albumin (BSA)), techniques of UV-visible, fluorescence, and circular dichroism (CD) spectroscopies are used. The binding affinity is more in case of PMZ with both the serum albumins. The quenching rate constant (k(q)) values suggest a static quenching process for all the drug-serum albumin interactions. The UV-visible results show that the change in protein conformation of PMZ-serum albumin interactions are more prominent as compared to NOT-serum albumin interactions. The CD results also explain the conformational changes in the serum albumins on binding with the drugs. The increment in %α-helical structure is slightly more for drug-BSA complexes as compared to drug-HSA complexes.
authors: Department of Chemistry, Aligarh Muslim University, Aligarh 202002, India.
authors: Abbul Bashar
authors: AB
authors: Khan
authors: Javed Masood
authors: JM
authors: Khan
authors: Mohd Sajid
authors: MS
authors: Ali
authors: Rizwan Hasan
authors: RH
authors: Khan
authors: Kabir-Ud-Din
mesh_terms: D000327:Adsorption; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D002942:Circular Dichroism; D006801:Humans; D007700:Kinetics; D009661:Nortriptyline / Q000737:chemistry / Q000378:metabolism*; D004364:Pharmaceutical Preparations / Q000737:chemistry / Q000378:metabolism*; D011395:Promazine / Q000737:chemistry / Q000378:metabolism*; D017433:Protein Structure, Secondary; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D013501:Surface-Active Agents / Q000737:chemistry / Q000378:metabolism*
chemical_list: D004364:Pharmaceutical Preparations; D013501:Surface-Active Agents; D012710:Serum Albumin, Bovine; D009661:Nortriptyline; D011395:Promazine