Burn-related Collagen Conformational Changes in ex vivo Porcine Skin using Raman Spectroscopy

Abstract

This 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.

Distinct Effects of Heparin and Interleukin‐4 Functionalization on Macrophage Polarization and In Situ Arterial Tissue Regeneration Using Resorbable Supramolecular Vascular Grafts in Rats

“…Amide I band topography gives insight into the secondary structure of complex proteins, depending on the contribution of the structural Raman peaks at 1635 and 1670 cm −1 to the profile of the amide I band. [ 35 ]…”

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“…Raman spectroscopy is emerging as a technique to characterize ECM, including the collagen of engineered and native cartilages, both in localized regions and throughout the entire tissue depth 81,82 . Raman spectroscopy has also recently been used to show changes in collagen secondary structure after damage from burning 83 and to discriminate between collagen types I and IV in skin 84 . TR-LIFS has been used to characterize collagen types I, II, III, IV and V in vitro 85 and was used to assess collagen type I in arterial plaques to diagnose atherosclerosis 86 .…”

Role of 3-Methacryloxypropyltrimethoxysilane in Dentin Bonding

“…The X-ray photoelectron spectroscopy (XPS) spectra, Fourier-transform infrared (FTIR) spectra, ultraviolet–visible (UV–vis) spectra, and Raman spectra of the pure collagen, collagen–MPS5, collagen–MPS10, and collagen–MPS15 are shown in Figure . The major peaks in Figure E,H correspond to type-I collagen. , Carbon, oxygen, and nitrogen peaks can be observed in the XPS spectra of all the sample surfaces. As shown in Figure G, collagen has two UV–vis absorption peaks at 212 and 282 nm .…”

“…The major peaks in Figure 1 E,H correspond to type-I collagen. 23 , 24 Carbon, oxygen, and nitrogen peaks can be observed in the XPS spectra of all the sample surfaces. As shown in Figure 1 G, collagen has two UV–vis absorption peaks at 212 and 282 nm.…”