Proteins show conformational changes on binding with ligands. Bovine serum albumin (BSA) is a plasma protein binds with a remarkable variety of ligands like drugs. To clarify the structural change of BSA–drug complexes UV and other spectroscopic studies are helpful. Fluphenazine is a antipsychotic drug, used in chronic psychoses treatment like schizophrenia. The present work explores the binding of fluphenazine with the bovine serum albumin (BSA) by UV-visible and fluorescence quenching spectra, synchronous fluorescence spectra measurement studies. Fluorescence intensity of BSA was quenched on increasing concentration addition of fluphenazine. BSA structure alteration by fluphenazine was shown by UV-vis and synchronous fluorescence studies. Change in stability of native BSA in presence of fluphenazine was studied by spectroscopic analysis. CD Spectra Measurements indicates change in BSA after binding with fluphenazine at secondary structure level. Molecular Docking results revealed that fluphenazine showed significant binding affinity towards the Sudlow‟s sites present within subdomain IIA of domain II and subdomain IIIB of domain III.