Abstract
Tip-enhanced Raman spectroscopy is a surface sensitive analytical method that combines the advantages of scanning probe microscopy and Raman spectroscopy. It holds great promises for imaging of biological samples with high spatial resolution (10–50 nm), well below the optical diffraction limit. It offers the opportunity to directly localize and identify proteins and their conformation in a complex (e.g., native) environment. Tip-enhanced Raman (TER) spectra in the so-called “gap-mode” configuration with a metal tip in scanning tunnelling feedback with a metal substrate coated with different proteins (bovine serum albumin, immunoglobulin G, trypsin, and β-lactoglobulin) as well as of model octapeptides (with and without an aromatic amino acid residue) are presented. The goal was to determine if it is possible to reliably assign marker bands for proteins and if different secondary structures of proteins can be distinguished in their gap-mode TER spectra as reliably as by IR and conventional Raman spectrosco...
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