The binding ability between 4-phenylbutan-2-amine (PBA) and Bovine Serum Albumin (BSA) was mainly investigated by UV-Visible and fluorescence spectroscopic methods. From the intensity of fluorescence spectra, it was observed that the 4-phenylbutan-2-amine has a strong ability to quench the intrinsic fluorescence of BSA through a static quenching mechanism. The binding constant and number of binding sites were investigated using Stern-Volmer equation. Conformation changes of BSA were observed from synchronous and Circular Dichroism (CD) spectra. The results of UV-Vis, CD, synchronous fluorescence spectral revealed the changes in the secondary structure of BSA upon interaction with 4-phenylbutan 2-amine thereby confirming their binding nature.