FT-Raman spectroscopic study of human skin subjected to uniaxial stress

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 1658cm−1 (amide I), 1271 and 1255cm−1 (amide III), and 935 and 817cm−1 (CC stretching modes of the protein backbone). Moreover, bands characteristic for amino acids were observed at 1336cm−1 (desmosine), 1004cm−1 (phenylalanine), 919 and 856cm−1 (proline), and 877cm−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. Direction-depending mechanical properties of human thigh skin were measured. Raman spectroscopy was used to investigate the molecular changes of structural proteins in a human skin subjected to a uniaxial strain. It has been found that collagen and elastin fibres are responsible for skin strength and molecular mechanism for load transferring has been proposed. [Display omitted] ► Mechanical properties of human thigh skin were investigated. ► Uniaxial tensile tests were performed depending on skin cutting direction. ► Raman scattering studies revealed structural changes under stress. ► A molecular mechanism for load transferring by proteins was proposed.