Molecular and fibrillar structure collagen analysis by FTIR spectroscopy

Abstract

Abstract The main component of connective tissue and human organs — collagen protein is widely used in tissue engineering, regenerative medicine and cosmetology. The new methods search for assessing the structural and qualitative characteristics of collagen is currently an urgent area. This research is devoted to analyze by FTIR spectroscopy the various structural forms of collagen during the transition from molecular to fibrillar form and also collagen fibrils destruction. It was shown that during the formation of fibrils in the IR spectra, a peak arise with a wavenumber of 1083 cm−1. The magnitude of this peak can be used to judge the degree of fibrillation of molecular collagen in vitro. It was shown that the addition of a hydrogen peroxide solution with concentrations of 0.6, 1.5, and 3% in the initial solution with fibrillar collagen leads to the destruction of fibrils, which manifests itself in a noticeable fading of the peak with a wavenumber of 1083 cm−1.