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Molecular interaction of some cardiovascular drugs with human serum albumin at physiological-like conditions: A new approach.

Authors :
Niaei N
Hasanzadeh M
Shadjou N
Source :
Journal of molecular recognition : JMR [J Mol Recognit] 2018 Aug; Vol. 31 (8), pp. e2715. Date of Electronic Publication: 2018 Apr 06.
Publication Year :
2018

Abstract

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.<br /> (Copyright © 2018 John Wiley & Sons, Ltd.)

Details

Language :
English
ISSN :
1099-1352
Volume :
31
Issue :
8
Database :
MEDLINE
Journal :
Journal of molecular recognition : JMR
Publication Type :
Academic Journal
Accession number :
29630759
Full Text :
https://doi.org/10.1002/jmr.2715