Investigations of the Interaction Mechanism Between Orphenadrine Hydrochloride and Bovine Serum Albumin by Spectroscopic and Voltammetric Techniques

• Published in: Journal of fluorescence 2023-09, Vol.33 (5), p.2061-2073
• Main Authors: Gokavi, Naveen M., Nandibewoor, Sharanappa T., Gowda, Jayant I.
• Format: Article
• Language: English
• Subjects: Alternations; Analytical Chemistry; Binding sites; Biochemistry; Biological and Medical Physics; Biomedical and Life Sciences; Biomedicine; Biophysics; Biotechnology; Calcium ions; Cattle; Cobalt; Fluorescence; Fourier transforms; Infrared spectra; Infrared spectroscopy; Investigations; Proteins; Quenching; Serum albumin; Spectrum analysis
• ISSN: 1053-0509; 1573-4994
• DOI: 10.1007/s10895-023-03199-y

The interaction of orphenadrine hydrochloride (ORD) with the model protein, bovine serum albumin (BSA), was investigated using a variety of spectroscopic techniques such as steady-state fluorescence, ultraviolet–visible, Fourier transform infrared, 3-D spectroscopy, and electrochemical methods under physiological conditions. Stern–Volmer plots were used to calculate fluorescence quenching at various temperatures. The findings point to a static quenching mechanism between ORD and BSA. At various reaction times, the binding sites (n) and binding constants (K) of ORD to BSA were recorded. Thermodynamic parameters ∆H 0 , ∆S 0 and ∆G 0 between ORD and BSA were calculated and reported. The average binding distance (r) between the donor (BSA) and acceptor (ORD) molecules was predicted using Förster's theory. Three-dimensional fluorescence spectra, Fourier transform infrared spectra, and synchronous fluorescence studies all supported the alternations in protein structure following the interaction with ORD. A displacement study using site probes such as warfarin, ibuprofen, and digitoxin confirmed ORD binding at Sudlow's site I of BSA. The effect of common metal ions such as Cu 2+ , Ni 2+ , Ca 2+ , Co 2+ , and Zn 2+ on binding constant values was investigated and reported.