Probing Biomolecule-Surface Interactions with Surface-Enhanced Raman Spectroscopy

Abstract

Surface-enhanced Raman (SER) spectroscopy is a powerful tool for characterizing the interactions of peptides and proteins with metal sur faces. Systematic studies on small biomolecules provide insights into the relative importance of specific functional groups and conformational con straints in determining the orientations and conformations of these molecules at metal-water interfaces, and provide the basis for understanding and predict ing the interfacial behavior of proteins. Changes in the conformations of globu lar proteins in contact with colloidal silver occur on the same time scale as has been observed by total internal reflection fluorescence and attenuated total reflectance infrared spectroscopy, but SER spectroscopy also reveals details of the protein-metal interactions. Methods for extending SER spectroscopy to the characterization of biopolymer surfaces are noted.