The interaction between benzylidene piperidone (BzP) and bovine serum albumin (BSA) was investigated by spectroscopic techniques. It was observed that BzP has a strong ability to quench the intrinsic fluorescence of BSA through static quenching. The binding constant 'K' and number of binding sites 'n' were calculated, and Gibbs free energy [ΔG0] change was found to be negative. The negative ΔG0 values confirmed that the binding process is spontaneous. The conformation changes of BSA investigated by synchronous, and circular dichroism spectra revealed the changes in the secondary structure of BSA upon interaction with BzP. Synchronous fluorescence spectra showed a change from red to blue shift which is an indication of increasing hydrophobicity.