RESUMO
Fourier Transform Raman Spectroscopy was used to investigate the molecular changes of structural proteins in human skin subjected to strain. In the Raman spectrum of unstrained skin, bands assigned mainly to collagen and elastin were observed at 1658 cm(-1) (amide I), 1271 and 1255 cm(-1) (amide III), and 935 and 817 cm(-1) (C-C stretching modes of the protein backbone). Moreover, bands characteristic for amino acids were observed at 1336 cm(-1) (desmosine), 1004 cm(-1) (phenylalanine), 919 and 856 cm(-1) (proline), and 877 cm(-1) (hydroxyproline). Positions and intensities of the listed Raman bands were analysed as a function of applied strain. A clear correlation between Raman wavenumbers and the level of mechanical stress was established. Wavenumbers of the analysed bands changed gradually with increasing strain. Distinct responses, depending on the sample cutting direction, i.e. longitudinal or perpendicular to the Langer's lines, were noticed. It was concluded that elastin and non-helical domains of collagen are initially involved in the load transfer and triple helices of collagen are gradually joining this process. It was proved that Raman spectroscopy give insight into skin deformation micromechanics.