• Hanglin Ye, Rahul Center for Modeling, Simulation and Imaging in Medicine (CeMSIM), Rensselaer Polytechnic Institute, Troy, NY, USA., Uwe Kruger, Tianmeng Wang, Sufei Shi, Jack Norfleet, and Suvranu De.
• Center for Modeling, Simulation and Imaging in Medicine (CeMSIM), Rensselaer Polytechnic Institute, Troy, NY, USA.
• Sci Rep. 2019 Dec 16; 9 (1): 19138.

AbstractThis study utilizes Raman spectroscopy to analyze the burn-induced collagen conformational changes in ex vivo porcine skin tissue. Raman spectra of wavenumbers 500-2000 cm-1 were measured for unburnt skin as well as four different burn conditions: (i) 200 °F for 10 s, (ii) 200 °F for the 30 s, (iii) 450 °F for 10 s and (iv) 450 °F for 30 s. The overall spectra reveal that protein and amino acids-related bands have manifested structural changes including the destruction of protein-related functional groups, and transformation from α-helical to disordered structures which are correlated with increasing burn severity. The deconvolution of the amide I region (1580-1720 cm-1) and the analysis of the sub-bands reveal a change of the secondary structure of the collagen from the α-like helix dominated to the β-aggregate dominated one. Such conformational changes may explain the softening of mechanical response in burnt tissues reported in the literature.

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