Structure and physico-chemical properties of fibrillary collagen fabric modified by silicon dioxide and hyaluronic acid

The connective tissue sheaths of paravertebral tendons (peritenons) of white laboratory rats treated with silicon dioxide and hyaluronic acid were studied. It was found that peritenones are natural composites with orthogonal anisotropy with a developed system of interstitial porous membranes that regulate tissue hydrodynamic flows. The extracellular matrix of peritenons contains carbonate-hydroxyapatite and calcium hydroxide in the amorphized state. Silicon dioxide and hyaluronate form hydrophobic silicate and hyaluronate coatings of collagen fibrils (encapsulation), strengthen bonds in Amides I, II, III, reduce the intensity of the bands of bound hydroxyl and stretching vibration bands of phosphate groups, which indicates the replacement of OH groups with carbonate ions and the suppression synthesis of hydroxyapatite. A key mechanism for reducing the intensity of apatitogenesis is the encapsulation of collagen fibrils, accompanied by screening the centers of epitaxial interactions that are structured during heterogeneous nucleation of calcium phosphates. In SBF biomimetic fluid, the deforming effect of modifying agents is leveled, but hydration and decomposition of fibrillar collagen increase. Moreover, against the background of excess supply of exogenous phosphates and carbonates from SBF, apatitogenesis in peritenons is carried out mainly by the mechanism of homogeneous nucleation.

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