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, UV-visible, Fourier transform IR, 3-D spectroscopy, and electrochem. methods under physiol. conditions.Stern-Volmer plots were used to calculate fluorescence quenching at various temperaturesThe 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.Thermodn. parameters ΔH0, ΔS0 and ΔG0 between ORD and BSA were calculated and reported.The average binding distance (r) between the donor (BSA) and acceptor (ORD) mols. was predicted using Forster's theory.Three-dimensional fluorescence spectra, Fourier transform IR 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 Cu2+, Ni2+, Ca2+, Co2+, and Zn2+ on binding constant values was investigated and reported.