Competitive binding effects on surface-enhanced Raman scattering of peptide molecules.
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.
Seballos
Leo
L
Department of Chemistry and Biochemistry, University of California, Santa Cruz, CA 95064, USA.
Richards
Nicole
N
Stevens
Daniel J
DJ
Patel
Mira
M
Kapitzky
Laura
L
Lokey
Scott
S
Millhauser
Glenn
G
Zhang
Jin Z
JZ