Abstract
Abnormal formation and organization of collagen network is commonly observed in many organ pathologies, but analytical techniques able to reveal the collagen biodistribution are still lacking. In this study, Fourier-transform infrared (FTIR) spectroscopy has been used to analyze type I, III, IV, V, and VI collagens, the most important compounds of connective tissues. A robust classification of 30 FTIR spectra per collagen type could be obtained by using a combination of four spectral intervals [nu(C=O) absorption of amide I (1,700-1,600 cm(-1)), delta(CH(2)), and delta(CH(3)) absorptions (1,480-1,350 cm(-1)), nu(C-N), and delta(N-H) absorptions of amide III (1,300-1,180 cm(-1)), and nu(C-O) and nu(C-O-C) absorptions of carbohydrate moieties (1,100-1,005 cm(-1))]. Then, a submolecular justification of this classification model was sought using a curve fitting analysis of the four spectral intervals. Results demonstrated that every spectral interval used for the classification contained highly discriminant absorption bands between all collagen types (multivariate analysis of variance, p < 0.01; Dunnett's T3 post hoc test, p < 0.05). All conditions seem thus joined to make FTIR spectroscopy and imaging major tools for implementing innovative methods in the field of molecular histology, which would be very helpful for the diagnosis of a wide range of pathologies.