Effect of Chitosan Deacetylation on Its Affinity to Type III Collagen: A Molecular Dynamics Study

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.

Collagen type II–hyaluronan interactions – the effect of proline hydroxylation: a molecular dynamics study

“…The formation of ionic interactions is typical for collagen–glycosaminoglycan systems. 106 However, due to the presence of several basic/acidic centers and zwitterionic residues character, different kinds of interactions can potentially be formed. In Fig.…”

Hydrated Collagen: Where Physical Chemistry, Medical Imaging, and Bioengineering Meet

“…Collagen has been well-known for some time to exhibit electromechanical coupling, which has been demonstrated to be the principal contributor to the piezoelectricity of bone and tendon. Several groups have endeavored to experimentally measure the piezoelectric tensor at the molecular level and to understand the molecular basis of collagen piezoelectricity, paving the way toward applications of this phenomenon to tissue engineering and biosensing. , Understanding of collagen interactions with other biological macromolecules is crucial to the development of biomimetic materials for a wide range of uses, including tissue regeneration, drug delivery, 3D printing, implant coating, and even cosmetic applications. , Similarly, understanding of the interfacial properties of collagen can provide further insights into the function of articular cartilage and is crucial to the development of novel materials for surgical implants. , Understanding of collagen–water interactions also has implications for the development of noncollagen-based nanomaterials . Finally, understanding of the interaction of collagen with proteolytic enzymes, particularly matrix metalloproteinases, has important implications for the development of biomaterials and can provide insights into degenerative diseases of articular cartilage.…”

Atomic-Resolution Experimental Structural Biology and Molecular Dynamics Simulations of Hyaluronan and Its Complexes

“…Small hyaluronan fragments were determined to be especially capable of decreasing the rate of water permeation through the transmembrane water channel aquaporin-3, which may be relevant to the mechanisms by which hyaluronan can moisturize skin [ 182 ]. Molecular dynamics simulations have been applied to compare the capacity of chitosan vs. hyaluronan to bind to collagen [ 183 ]. MM-GBSA post-processing of simulation trajectories of hyaluronan with five different cathepsin proteins showed a ~15 kcal/mol range in binding affinity based on the cathepsin type and the hyaluronan length, with the binding affinity showing either a direct, an inverse, or no correlation with hyaluronan length depending on the cathepsin type [ 184 ].…”