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Molecular interaction of some cardiovascular drugs with human serum albumin at physiological‐like conditions: A new approach
Author(s) -
Niaei Navid,
Hasanzadeh Mohammad,
Shadjou Nasrin
Publication year - 2018
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.2715
Subject(s) - human serum albumin , quenching (fluorescence) , chemistry , fluorescence , hydrophobic effect , fluorescence spectroscopy , fourier transform infrared spectroscopy , biophysics , atenolol , static electricity , biochemistry , biology , chemical engineering , physics , quantum mechanics , blood pressure , engineering , endocrinology , electrical engineering
In the present study, the interaction of human serum albumin (HSA) with some cardiovascular drugs (CARs) under physiological conditions was investigated via the fluorescence spectroscopic and Fourier transform infrared spectroscopy. The CAR included Captopril, Timolol, Propranolol, Atenolol, and Amiodarone. Cardiovascular drugs can effectively quench the endogenous fluorescence of HSA by static quenching mechanism. The fluorescence quenching of HSA is mainly caused by complex formation of HSA with CAR. The binding reaction of CAR with HSA can be concluded that hydrophobic and electrostatic interactions are the main binding forces in the CAR‐HSA system. The results showed that CAR strongly quenched the intrinsic fluorescence of HSA through a static quenching procedure, and nonradiation energy transfer happened within molecules. Fourier transform infrared spectroscopy absorption studies showed that the secondary structure was changed according to the interaction of HSA and CAR. The binding reaction of CAR with HSA can be concluded that hydrophobic and electrostatic interactions are the main binding forces in the CAR‐HSA system. The results obtained herein will be of biological significance in pharmacology and clinical medicines.