Abstract
The parameters of the condensed state and structure of fibrillar collagen and the composition and structuring of calcium phosphates in collagen gel samples obtained from rat tail tendons were studied. After the acid extraction and gelation at 37°С, fibrillar collagen preserves the domain organization and undergoes dispersion to the subfibrillar level and aggregation; the extrafibrillar space is filled with a viscous liquid. The dilatancy arises at 37–40°С at low and medium shear stresses and rates. In the course of acid extraction, fibrillar collagen undergoes amorphization, its primary peptide chains are hydrated and undergo heterogeneous strengthening/softening; the interchain spaces undergo contraction/expansion. Calcium phosphates originating from the initial tendons and medium 199 undergo structuring into hydroxyapatites in the course of gelation. These hydroxyapatites undergo decarbonation on introducing hyaluronic acid and become close to hydroxyapatite Са10(РО4)6(ОН)2 in the structure. The gels treated with hyaluronic acid form strong networks and fibrillar nodes of increased connection, shifting the dilatancy toward higher shear rates and stresses. Collagen fibers undergo aggregation to form thickened platelike structures tending to exfoliation. The water-filled interfibrillar spaces are expanded. Hyaluronic acid prevents the amorphization of fibrillar collagen, reduces the intermolecular contact strength, and suppresses the growth of hydroxyapatite structural precursors.
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ACKNOWLEDGMENTS
The study was performed using the equipment of the Lykov Institute of Heat and Mass Exchange, National Academy of Sciences of Belarus, and Institute of Cytology, Russian Academy of Sciences.
The authors are grateful to Cand. Sci. (Eng.) T.A. Kuznetsova and Head of Laboratory of Nanoprocesses and Technologies Dr. Sci. (Eng.) S.A. Chizhik for the assistance in performing atomic force microscopy and to Cand. Sci. (Biol.) L.V. Kukhareva and Cand. Sci. (Biol.) Yu.A. Nashchekina for the preparation of the collagen solution and gel.
Funding
The study was financially supported by the State Research Program “Chemical Processes, Reagents, and Technologies, Bioregulators, and Bioorganic Chemistry,” task 2.1.04.7, for the years 2021–2025 (Institute of General and Inorganic Chemistry, National Academy of Sciences of Belarus; Research Institute for Physicochemical Problems, Belarusian State University; Lykov Institute of Heat and Mass Exchange, National Academy of Sciences of Belarus), and by the Ministry of Science and Higher Education of the Russian Federation within the framework of government assignment no. FMFU-2021-0008 (Institute of Cytology, Russian Academy of Sciences).
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A.A. Gaidash: development of the methodology for preparing samples of tendons, collagen extracts, and gels and for studying them by IR spectroscopy, analysis of the data of scanning and atomic force microscopy, writing of the paper, and literature search; V.K. Krut’ko: participation in experiments on treatment of the samples with hyaluronic acid and determination of the phase composition; O.N. Musskaya: rheological study; O.A. Sycheva: thermal analysis; L.V. Kul’bitskaya: IR spectroscopy; G.B. Mel’nikova: atomic force microscopy; K.V. Skrotskaya: scanning electron microscopy; M.I. Blinova: experiments on preparation of collagen extracts and gels; A.I. Kulak: formulation of the research tasks and goal.
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Translated from Zhurnal Prikladnoi Khimii, Nos. 11–12, pp. 1424–1438, August, 2022 https://doi.org/10.31857/S004446182211007X
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Gaidash, A.A., Krut’ko, V.K., Musskaya, O.N. et al. Structure and Physicochemical Properties of Collagen Gels Treated with Hyaluronic Acid. Russ J Appl Chem 95, 1701–1714 (2022). https://doi.org/10.1134/S1070427222110039
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DOI: https://doi.org/10.1134/S1070427222110039