The effects of anticalcification treatments and hydration on the molecular dynamics of bovine pericardium collagen as revealed by 13C solid-state NMR

• Published in: Magnetic resonance in chemistry Vol. 48; no. 9; pp. 704 - 711
• Main Authors: deAzevedo, E. R., Ayrosa, A. M. I. B., Faria, G. C., Cervantes, H. J., Huster, D., Bonagamba, T. J., Pitombo, R. N. M., Rabbani, S. R.
• Format: Journal Article
• Language: English
• Published: Chichester, UK John Wiley & Sons, Ltd 01.09.2010
• Subjects: 13C; Animals; bovine pericardium; Carbon Isotopes; Cattle; collagen; Collagen - chemistry; glutaraldehyde; heart valve prostheses; Magnetic Resonance Spectroscopy - standards; Molecular Dynamics Simulation; Molecular Structure; NMR; Pericardium - chemistry; phenetylamine-diepoxide; Reference Standards
• ISSN: 0749-1581; 1097-458X
• DOI: 10.1002/mrc.2653

This article describes a solid‐state NMR (SSNMR) investigation of the influence of hydration and chemical cross‐linking on the molecular dynamics of the constituents of the bovine pericardium (BP) tissues and its relation to the mechanical properties of the tissue. Samples of natural phenetylamine‐diepoxide (DE)‐ and glutaraldehyde (GL)‐fixed BP were investigated by 13C cross‐polarization SSNMR to probe the dynamics of the collagen, and the results were correlated to the mechanical properties of the tissues, probed by dynamical mechanical analysis. For samples of natural BP, the NMR results show that the higher the hydration level the more pronounced the molecular dynamics of the collagen backbone and sidechains, decreasing the tissue's elastic modulus. In contrast, in DE‐ and GL‐treated samples, the collagen molecules are more rigid, and the hydration seems to be less effective in increasing the collagen molecular dynamics and reducing the mechanical strength of the samples. This is mostly attributed to the presence of cross‐links between the collagen plates, which renders the collagen mobility less dependent on the water absorption in chemically treated samples. Copyright © 2010 John Wiley & Sons, Ltd. Solid‐state NMR was used to investigate the influence of hydration and chemical cross‐linking on the molecular dynamics of the bovine pericardium collagen. The results show that the degree of molecular dynamics in the collagen backbone and sidechain are affected by the presence of chemical cross‐linking and hydration also affecting the elastic modulus of pericardium tissue.