Steady-state and time-resolved fluorescence spectroscopic study on the interaction between bovine serum albumin and Ag-nanoparticles

The interaction between bovine serum albumin(BSA) and Ag-nanoparticles was studied under a pH 7.4 buffer system by time-resolved fluorescence technique combined with the steady-state absorption and fluorescence spectrum. With Ag-nanoparticles, the BSA showed blue shift of fluorescence from 335nm to 332.5nm, accompanied by the fluorescence intensity decreasing. When adding the Ag-nanoparticles to the three fluorescent amino acids tryptophan(Trp), tyrosine(Tyr) and phenylalanine(Phe), only Trp displayed peak shift which from 346.5nm to 341nm. Strong interaction between BSA and the Ag-nanoparticles may come from Trp residue. Time-resolved fluorescence gave that BSA had only one fluorescence lifetime around 6ns from 308 to 313K. When adding Ag-nanoparticles, two fluorescence lifetimes appeared. One is a little above than 6ns and the other is around 3ns. The two Trp residues in 134th and 212th position may give contribution to the changes of the fluorescence lifetime. The 134th Trp residue is probably protected by BSA molecule structure and basically don't contact with Ag-nanoparticles, which shows little change of fluorescence lifetime. The 212th Trp residue is likely the target of the Ag-nanoparticles. The Ag-nanoparticles changed the microenvironment of BSA around the 212th Trp residue and therefore increases the exposure of the 212th Trp and the 134th Trp.