(2017) Exploring isoxsuprine hydrochloride binding with human serum albumin in the presence of folic acid and ascorbic acid using multispectroscopic and molecular modeling methods. Journal of Photochemistry and Photobiology B-Biology. pp. 152-163. ISSN 1011-1344
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Abstract
Isoxsuprine hydrochloride (vasodilator drug), folic acid and ascorbic acid are medicines which can be utilized alone or simultaneously by pregnant women. In the present work the competitive binding of isoxsuprine hydrochloride (ISO) with human serum albumin (HSA) in the absence and presence of folic acid (FOL) and ascorbic acid (AS) was investigated using different spectroscopic probes and molecular docking studies. The results of fluorescence suggested that isoxsuprine alone or in the presence of ascorbic acid can bind to HSA and quench the fluorescence of HSA with static mechanism but For HSA-folic acid-isoxsuprine system, dynamic type of quenching mechanisms is involved. The values of binding constants (KHSA-ISO similar to 1.2 X 10(3) M-1, KHSA-AS-ISO similar to 2.1 x 10(3) M-1 land KHSA-FOL-ISO similar to 0.7 x 10(3) M-1) suggested that affinity of HSA to isoxsuprine increased in the presence of ascorbic acid while the presence of folic acid reduced the affinity of protein to isoxsuprine. The results of FT-IR and circular dichroism measurements indicated that the binding of isoxsuprine to HSA in the absence and the presence of folic acid and ascorbic acid may induce conformational and microenvironmental changes of protein. Not only do these types of spectroscopy techniques provide all the information about the systems, molecular docking, also emphasizes the results and is employed for the identification of the active site residues, bioactive conformer of Isoxsuprine and their critical interactions.
Item Type: | Article |
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Keywords: | isoxsuprine hydrochloride ascorbic acid folic acid human serum albumin interaction spectroscopic studies molecular docking fluorescence spectroscopy fluoxetine hydrochloride complexes proteins affinity docking sites drugs labor |
Divisions: | |
Page Range: | pp. 152-163 |
Journal or Publication Title: | Journal of Photochemistry and Photobiology B-Biology |
Volume: | 170 |
Identification Number: | 10.1016/j.jphotobiol.2017.04.007 |
ISSN: | 1011-1344 |
Depositing User: | مهندس مهدی شریفی |
URI: | http://eprints.zbmu.ac.ir/id/eprint/2410 |
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