Modification of the Collagen Tissue of the Bioprothesis of Heart Valves in a Solution of Carbonic Acid: Effect of Pressure on Adsorption of Chitosan and the Structure of the Tissue

Abstract:

For the first time the influence of pressure of chitosan solutions in carbonic acid on the adsorption of chitosan onto a collagen tissue of biological heart-valve prostheses and on the structure of the resulting biocomposite was studied. It turned out that the dependence of an amount of the chitosan adsorbed onto the collagen tissue has bell-shaped form reaching a maximum adsorption of about 0.8 weight. % at 30-40 MPa and then falling to 0.3 wt. % with further pressure increase up to 50 MPa. It was found that this treatment leads to a significant change of the morphology of the tissue surface which depends on the pressure in the system. It was also revealed that under pressure growth collagen fibrils are compacted in the tissue bulk which leads to the extrusion of the polymer embedded in the collagen matrix.

• Periodical: Materials Science Forum (Volume 935)
• Pages: 100-107
• DOI: https://doi.org/10.4028/www.scientific.net/MSF.935.100
• Online since: October 2018
• Authors: I.S. Chaschin, N.P. Bakuleva, M.G. Chernysheva, G.A. Badun, N.M. Anuchina, S.S. Abramchuk, L.N. Nikitin
• Keywords: Adsorption, Biological Heart-Valve Prostheses, Bovine Pericardium, Carbonic Acid, Chitosan, Collagen Tissue, Pressure

References

[1] S. C. Cannegieter, F. R. Rosendaal, E. Briët, Thromboembolic and bleeding complications in patients with mechanical heart valve prostheses, J. Circulation. 89 (1994) 635–641.

DOI: 10.1161/01.cir.89.2.635

[2] P. D. Stein, J. S. Alpert, H. I. Bussey, J. E. Dalen, A. G. G. Turpie, Antithrombotic therapy in patients with mechanical or biological prosthetic heart valves, J. Chest. 119 (2001) 220–227.

DOI: 10.1378/chest.119.1_suppl.220s

[3] R. F. Siddiqui, J. R. Abraham, J. Butany, Bioprosthetic heart valves: modes of failure, J. Histopathology. 55 (2001) 135–144.

DOI: 10.1111/j.1365-2559.2008.03190.x

[4] F. J. Schoen, J. W. Tsao, R. J. Levy, Calcification of bovine pericardium used in cardiac valve bioprostheses, Am. J. Pathol. 123 (1986) 134–145.

[5] J. Chanda, Anticalcification treatment of pericardial prostheses, Biomaterials. 15 (1994) 465–469.

DOI: 10.1016/0142-9612(94)90226-7

[6] G. Nogueira, A. Rodas, R. Weska, C. Aimoli, O. Higa, M. Maizato, A. Leiner, R. Pitombo, B. Polakiewicz, M. Beppu, Bovine pericardium coated with biopolymeric films as an alternative to prevent calcification: in vitro calcification and cytotoxicity results, Mater. Sci. Eng.C. 30 (2010).

DOI: 10.1016/j.msec.2010.02.011

[7] M. O. Gallyamov, I. S. Chaschin, M. A. Khokhlova, T. E. Grigorev, N. P. Bakuleva, I. G. Lyutova, J. E. Kondratenko, G. A. Badun, M. G. Chernysheva, A. R. Khokhlov, Collagen tissue treated with chitosan solutions in carbonic acid for improved biological prosthetic heart valves, Mater. Sci. Eng. C. 37 (2014).

DOI: 10.1016/j.msec.2014.01.017

[8] G. A. Badun, M. G. Chernysheva, A. L. Ksenofontov, Increase in the specific radioactivity of tritium-labeled compounds obtained by tritium thermal activation method, Radiochim. Acta. 100 (2012) 401–408.

DOI: 10.1524/ract.2012.1926

[9] A. S. Kashin, V. P. Ananikov, A SEM study of nanosized metal films and metal nanoparticles obtained by magnetron sputtering, Russ. Chem. Bull. 60 (2011) 2602–2607.

DOI: 10.1007/s11172-011-0399-x

[10] M. H. Santos, R. M. Silva, V. C. Dumont, J. S. Neves, H. S. Mansur, L. G. D. Heneine, Extraction and characterization of highly purified collagen from bovine pericardiumfor potential bioengineering applications, Mater. Sci. Eng. C. 33 (2013).

DOI: 10.1016/j.msec.2012.11.003

[11] W. Sun, M. Sacks, G. Fulchiero, J. Lovekamp, N. Vyavahare, M. Scott, Response of heterograft heart valve biomaterials to moderate cyclic loading, J. Biomed. Mater. Res. 69 (2004) 658–669.

DOI: 10.1002/jbm.a.30031

[12] F. G. Pearson, R. H. Marchessault, C. Y. Liang, Infrared spectra of crystalline polysaccharides. V. Chitin, J. Polym. Sci. 43 (1960) 101–116.

DOI: 10.1002/pol.1960.1204314109

[13] D. J. S. Hulmes, Building collagen molecules, fibrils, and suprafibrillar structures, J. Struct. Biol. 137 (2002) 2–10.

DOI: 10.1006/jsbi.2002.4450

[14] G. S. Al-Saidi, A. Al-Alawi, M. S. Rahman, N. Guizani, Fourier transform infrared (FTIR) spectroscopic study of extracted gelatin from shaari (Lithrinusmicrodon) skin: effects of extraction conditions, Int. Food Res. 19 (2012) 1167—1173.

DOI: 10.1007/s10973-010-1240-8