A Raman Study of MMP2 and MnSOD, Two Pathology Biomarkers
Résumé
Matrix Metalloproteinases (MMPs) are cell-secreted soluble and membranetethered enzymes that degrade extracellular matrix (ECM) proteins. These proteases play a key role in diverse physiological and pathological processes, including embryonic development, wound repair, inflammatory diseases and cancer [1]. On the other hand, Superoxide Dismutases (SODs) are metalloenzymes that defend biological systems against oxidative damage mediated by the superoxide anion [2]. The vibrational spectra of MMPs and SODs can provide crucial information about conformational changes induced by external factors, e.g. the interaction with metal ions, drugs, others proteins or peptides. On the other side, Raman spectroscopy can be used as a tool for non-invasive and non-ambiguous spectral detection of these proteins at very low concentration (10-8-10-12 M), with potential applications in early diseases diagnosis [3]. At present, there is still insufficient knowledge on the Raman spectral fingerprints of these proteins. Here we present a complete Raman analysis of MMP2 and MnSOD using multiwavelength-excitation at 514, 633, and 785 nm.