Unraveling the Role of Hydroxyproline in Maintaining the Thermal Stability of the Collagen Triple Helix Structure Using Simulation

Abstract

The thermal stability of collagen has an important effect on its practical applications. Many believe that hydroxyproline (Hyp) improves the structural stability of collagen molecules. In this study, for the first time, a method of building natural collagen molecular models was described. We constructed a collagen model with typical triple-helix structure and calculated the hydrogen bond energy between collagen α chains. The calculated hydrogen bond energy was consistent with the experimental results of differential scanning calorimetry. After the calculation simulation, we verified that the hydrogen bond energy between collagen chains was positively correlated with Hyp content in the models and an increased Hyp content in the model was beneficial in improving the thermal resistance of the structure. In addition, we found that thermal unfolding did not occur simultaneously along the entire molecule but started in the regions with less Hyp content. This study provides a collagen model with a natural collagen amino acid sequence, which will be helpful for further investigation of the physical and chemical properties of natural collagen.

Factors affecting thermal stability of collagen from the aspects of extraction, processing and modification

“…For the first time, collagen model fragments with natural amino acid sequences were constructed by Li and her group [131] using computer simulation. To further study the effect of Hyp content on thermal stability of collagen molecules, the fragments of grass carp collagen were selected according to the distribution of Hyp content in diverse regions of amino acid sequences.…”

Mapping the metabolomic and lipidomic changes in the bleomycin model of pulmonary fibrosis in young and aged mice

“…The most abundant amino acids in collagen are glycine and proline, building the repeating motif Gly-Pro-X, where X can be any other amino acid ( Shoulders and Raines, 2009 ). Proline on certain positions is hydroxylated into hydroxyproline, which enables formation of the triple helix and renders increased thermal stability of collagen ( Xu et al, 2019 ). We found glycine to be the sole amino acid not significantly increased upon bleomycin treatment compared to controls ( Fig.…”

Characterization of Collagen from Three Genetic Lines (Gray, Red and F1) of Oreochromis niloticus (Tilapia) Skin in Young and Old Adults

“…The viscosity evaluations of the F1 fish at the ages of 9, 24, and 36 months showed the same tendency of a drastic decrease in the τd above 30 °C, being lower than the τd in the collagen PSC obtained from 36-month-old fish. Due to the effect of high temperatures, collagens change their triple helix structure and fragment into molecules of lower molecular weight [ 11 ]. Investigations of τd in tilapia according to age have not previously been evaluated.…”

“…It also ensures sustainability over time since its meat and skin are sources of collagen type I and other bioactive compounds [ 8 ]. This collagen is distinguished by its structural integrity stability, correlated with proline and hydroxyproline content [ 9 , 10 , 11 , 12 ].…”