Resonance Raman spectroscopy (RRS) is a promising technique for investigating samples with low concentrations of single constituents or many different constituents. The wavelength dependent resonance enhancement (resonance profile) of the respective molecule yields information about the targeted species and reveals the optimal wavelength for high resolution RRS. A significant increase of the Raman scattered intensity can already be achieved in the vicinity of the molecules' absorption band (preresonance). Measuring such preresonance and resonance profiles requires precise control of excitation conditions and careful assessment of the spectral accuracy of the setup. We present a comprehensive procedure for the acquisition of preresonance profiles in Raman spectroscopy. An experimental setup for recording the single spectra is combined with an efficient algorithm for data postprocessing. The procedure is demonstrated on amino acids measured in the UV and can be applied to any molecule and wavelength range.

Raman spectroscopy has proven to be an effective tool for molecular analysis in different applications. In clinical diagnostics, its application has enabled nondestructive investigation of biological tissues and liquids. The human perilymph, for example, is an inner ear liquid, essential for the hearing sensation. The composition of this liquid is correlated with pathophysiological parameters and was analyzed by extraction and mass spectrometry so far. In this work, we present a fiber optic probe setup for the Raman spectroscopic sampling of inner ear proteins in solution. Multivariate data analysis is applied for the discrimination of individual proteins (heat shock proteins) linked to a specific type of hearing impairment. This proof-of-principle is a first step toward a system for sensitive and continuous in vivo perilymph investigation in the future.

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