David Pérez-Guaita

In the last of a three-part series, Spectroscopy spoke to a team of researchers (including Katarzyna M. Marzec and Natalia Wilkosz, corresponding authors of the resulting paper) can track diabetes progression through spectral markers of protein aggregation and membrane rigidity, account for age- and sex-dependent variations in the db/db mouse model and address translational challenges in adapting murine spectrochemical signatures to human type 2 diabetes diagnostics.

In the second of a three-part series, Spectroscopy spoke to researchers (including Katarzyna M. Marzec and Natalia Wilkosz, corresponding authors of the resulting paper) about how FT-IR spectroscopy and Raman spectroscopy detect oxidative stress–related disulfide bond alterations and protein instability in diabetic RBCs, address experimental challenges in resolving membrane versus cytoplasmic protein signals, enable non-invasive molecular profiling beyond conventional assays, and, when coupled with multivariate tools such as oPLS-DA and VIP scoring, enhance robust identification of disease-specific spectral biomarkers.

Using Fourier transform infrared (FT-IR) spectroscopy and Raman spectroscopy, a research team identified sex- and age-specific molecular alterations in red blood cells from diabetic mice.In the first of a three-part series, Spectroscopy spoke to members of the research team (including Katarzyna M. Marzec and Natalia Wilkosz, corresponding authors of the resulting paper) about how FT-IR differentiates α-helix, β-sheet, and β-turn structures in RBC membrane proteins through analysis of the Amide I and Amide II bands—enhanced by second-derivative processing to reveal subtle protein misfolding in T2DM—while its complementary use with Raman spectroscopy provides a more comprehensive molecular assessment of protein conformation, lipid remodeling, and oxidative stress–induced membrane alterations.