Abstract
The ability to form strong intermolecular interactions by linear glucosamine polysaccharides with collagen is strictly related to their nonlinear dynamic behavior and hence bio-lubricating features. Type III collagen plays a crucial role in tissue regeneration, and its presence in the articular cartilage affects its bio-technical features. In this study, the molecular dynamics methodology was applied to evaluate the effect of deacetylation degree on the chitosan affinity to type III collagen. The computational procedure employed docking and geometry optimizations of different chitosan structures characterized by randomly distributed deacetylated groups. The eight different degrees of deacetylation from 12.5% to 100% were taken into account. We found an increasing linear trend (R2 = 0.97) between deacetylation degree and the collagen–chitosan interaction energy. This can be explained by replacing weak hydrophobic contacts with more stable hydrogen bonds involving amino groups in N-deacetylated chitosan moieties. In this study, the properties of chitosan were compared with hyaluronic acid, which is a natural component of synovial fluid and cartilage. As we found, when the degree of deacetylation of chitosan was greater than 0.4, it exhibited a higher affinity for collagen than in the case of hyaluronic acid.
Highlights
Many of the synovial joints’ diseases, such as degeneration and inflammation, are associated with the deficiency of essential components forming cartilage and synovial fluid
This study analyzed the intermolecular interactions between chitosan and collagen type III using molecular docking methodology followed by molecular dynamics simulations
A completely deacetylated chitosan (DD = 100%, Figure 2c) exhibits a parallel orientation in relation to collagen contrary to hyaluronic acid and chitosan–collagen complexes characterized by lower deacetylation degree (DD) values
Summary
Many of the synovial joints’ diseases, such as degeneration and inflammation, are associated with the deficiency of essential components forming cartilage and synovial fluid. These compounds are often classified as extracellular matrix molecules. The essential proteins belonging to this class, namely collagens, play the chief structural framework role in many tissues, including cartilage, tendons, skin, blood vessels, and bones. Collagen is a supramolecular system characterized by a triple helical structure. The collagen triple helices form the “building blocks” of tissues, namely fibrils and fibers. The capability of forming strong intermolecular interactions determines specific features of collagen, such as bio-compatibility, low antigenic activity, bio-degradability, and tissue regeneration abilities [3,4,5,6,7,8]
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