Instituto de Física de São Carlos, Universidade de São Paulo, Caixa Postal 369, 13560-970 São Carlos, SP, Brazil.
Magn Reson Chem. 2010 Sep;48(9):704-11. 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 phenethylamine-diepoxide (DE)- and glutaraldehyde (GL)-fixed BP were investigated by (13)C 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.
本文描述了固态核磁共振(SSNMR)对水合作用和化学交联对牛心包组织成分的分子动力学的影响的研究,以及其与组织力学性能的关系。通过(13)C 交叉极化 SSNMR 研究了天然苯乙胺-二环氧(DE)和戊二醛(GL)固定的 BP 样品,以探测胶原的动力学,结果与通过动态力学分析探测的组织力学性能相关联。对于天然 BP 样品,NMR 结果表明,水合水平越高,胶原主链和侧链的分子动力学越明显,从而降低组织的弹性模量。相比之下,在 DE 和 GL 处理的样品中,胶原分子更僵硬,并且水合作用在增加胶原分子动力学和降低样品机械强度方面的效果不那么明显。这主要归因于胶原板之间存在交联,这使得胶原的流动性较少依赖于化学处理样品中的水分吸收。