Spectroscopic investigations on the interaction of gabapentin (GBP) with bovine serum albumin (BSA) were reported. The association constant of GBP-BSA system was determined at different temperatures (298, 302, 306 and 311 K) based on the fluorescence quenching results. The GBP was found to quench the fluorescence of BSA through static mechanism. Thermodynamic parameters, the standard enthalpy change, $({Delta}H^o)$ and the standard entropy change $({Delta}S^o)$ were observed to be $-9.61{pm}0.008;kJ;mol^{-1}$ and $3.58{pm}0.011;Jmol^{-1}K{-1}$ respectively. These indicated that the hydrophobic and electrostatic forces played a role in the interaction of GBP with BSA. The negative value of ${Delta}G^o$ revealed that the binding reaction is spontaneous. The circular dichroism studies indicated the conformational changes in BSA upon interaction with GBP. The effect of some metal ions on the binding constant was also investigated.