Author/Authors :
S. and Seballos، نويسنده , , Leo and Richards، نويسنده , , Nicole and Stevens، نويسنده , , Daniel J. and Patel، نويسنده , , Mira and Kapitzky، نويسنده , , Laura and Lokey، نويسنده , , Scott and Millhauser، نويسنده , , Glenn and Zhang، نويسنده , , Jin Z.، نويسنده ,
Abstract :
Surface enhanced Raman scattering (SERS) has been conducted on tryptophan (W), proline (P) and tyrosine (Y) containing peptides that include W-P-Y, Y-P-W, W-P-P-P-Y, Y-P-P-P-W, W-P-P-P-P-P-Y, and Y-P-P-P-P-P-W to gain insight into molecular binding behavior on a metal substrate to eventually apply in protein SERS detection. The peptides are shown to bind through the molecule’s carboxylic end, but the strong affinity of the tryptophan residue to the substrate surface, in conjunction with its large polarizability, dominates each molecule’s SERS signal with the strong presence of its ring modes in all samples. These results are important for understanding SERS of protein molecules.
