Abstract
The binding of 1-chloro-3-(2-methyl-5-nitro-1H-imidazole-1-yl) propan-2-ol (Ornidazole) to human serum albumin (HSA) was studied by fluorescence and UV-visible spectroscopy. Interaction of ornidazole (OR) with HSA was identified by Stern-Volmer and Van’t Hoff equations. The binding constant, Kb and the thermodynamic parameters, ∆H, ∆S, and ∆G at different temperatures were calculated by several equations. Data shows that the fluorescence quenching mechanism of HSA with ornidazole may occur via static quenching. The thermodynamic parameters showed that van der Waals interactions and hydrogen bonds are the major forces for the interaction of ornidazole with HSA. The spectral changes of synchronous fluorescence suggested that both the microenvironment of OR and the conformation of HSA concerning their concentrations have changed during binding.  Â
Highlights
Albumin is the main protein for the transportation of a wide variety of substances like metals, fatty acids, amino acids, hormones, and a large list of drugs [1]
The blue shift means a decrease in the polarity of the microenvironment of OR. This result suggests that an interaction between OR and human serum albumin (HSA) occurs in the hydrophobic microenvironment of HSA
Our study shows that fluorescence spectroscopy can be very useful in investigating the molecular interactions between drugs and HSA
Summary
Albumin is the main protein for the transportation of a wide variety of substances like metals, fatty acids, amino acids, hormones, and a large list of drugs [1]. Albumin is widely used in the studies of interactions between drugs and proteins in vitro. Several types of albumin which are from human, rat, and bovine are the most commonly studied proteins to identify the interaction between proteins and drugs for many decades. The tridimensional structure is only available for human serum albumin (HSA). Ligands bind to two subdomains, IIA and IIIA in Sudlow site I and Sudlow site II These sites have hydrophobic cavities [5,6,7]. A large number of drugs and bioactive molecules bind reversibly to all types of albumin [8,9,10,11,12,13]. We demonstrated the binding of ornidazole to human serum albumin by using fluorescence and UV–Visible spectroscopy. This work aimed to determine the affinity of ornidazole to HSA and to investigate the thermodynamic parameters of their interaction
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