The interaction between silver nanoparticles (SNPs) and Bovine Serum Albumin (BSA) was investigated at physiological pH in an aqueous solution using fluorescence spectroscopy. The analysis of fluorescence spectrum and fluorescence intensity indicates that SNPs have a strong ability to quench the intrinsic fluorescence of BSA by both static and dynamic quenching mechanisms. Resonance light scattering (RLS) spectra indicated the formation of a complex between BSA and SNP. The number of binding sites 'n' and binding constants 'K' were determined at different temperatures based on fluorescence quenching. The thermodynamic parameters namely ∆H°, ∆G°, ∆S° were calculated at different temperatures and the results indicate that hydrophobic forces are predominant in the SNP-BSA complex. Negative ∆G° values imply that the binding process is spontaneous. Synchronous fluorescence spectra showed a blue shift which is indicative of increasing hydrophobicity.