【24h】

Thermal Properties of Mineralized and Non Mineralized Type I Collagen in Bone

机译:骨中矿化和非矿化的I型胶原蛋白的热学性质

获取原文
获取原文并翻译 | 示例

摘要

The research about the structural stability of bone, as a composite material, compromises a complete understanding of the interaction between the mineral and organic phases. The thermal stability of human bone and type 1 collagen extracted from human bone by different methods was studied in order to understand the interactions between the mineral and organic phases when is affected by a degradation/combustion process. The experimental techniques employed were calorimetry and infrared spectroscopy (FTIR) techniques. The extracted type I collagens result to have a bigger thermal stability with a Tmax at 500 and 530 Celsius degrees compared with the collagen present in bone with Tmax at 350 Celsius degrees. The enthalpy value for the complete degradation/combustion process were similar for all the samples, being 8.4 +- 0.11 kJ/g for recent bones diminishing with the antiquity, while for extracted collagens were 8.9 +- 0.07 and 7.9 +-1.01 kJ/g. These findings demonstrate that the stability loss of type 1 collagen is due to its interactions with the mineral phase, namely carbonate hydroxyapatite. This cause a change in the molecular properties of the collagen during mineralization, specifically in its cross-links and other chemical interactions, which have a global effect over the fibers elasticity, but gaining tensile strength in bone as a whole tissue. We are applying this characterization to analyze the diagenetic process of bones with archaeological interest in order to identify how the environmental factors affect the molecular structure of type I collagen. In bone samples that proceed from an specific region with the same environmental conditions, the enthalpy value per unit mass was found to diminish exponentially with respect to the bone antiquity.
机译:关于作为复合材料的骨骼的结构稳定性的研究损害了对矿物相和有机相之间相互作用的完整理解。研究了人类骨骼和通过不同方法从人类骨骼中提取的1型胶原蛋白的热稳定性,以了解受降解/燃烧过程影响的矿物相与有机相之间的相互作用。所采用的实验技术是量热法和红外光谱(FTIR)技术。与在350摄氏度下Tmax的骨骼中存在的胶原蛋白相比,提取的I型胶原蛋白具有更高的热稳定性(在500和530摄氏度下的Tmax)。对于所有样品,完全降解/燃烧过程的焓值相似,对于最近随着古代而减少的骨骼,其焓值为8.4 +-0.11 kJ / g,而对于提取的胶原蛋白,其焓值为8.9 +-0.07和7.9 + -1.01 kJ / g 。这些发现表明1型胶原蛋白的稳定性丧失是由于其与矿物质相即碳酸盐羟基磷灰石的相互作用。这会导致矿化过程中胶原蛋白的分子特性发生变化,尤其是其交联和其他化学相互作用的变化,这些变化对纤维的弹性具有全局性影响,但在整个骨组织中却具有抗张强度。我们正在应用此特征来分析具有考古学意义的骨骼的成岩过程,以便确定环境因素如何影响I型胶原的分子结构。在从具有相同环境条件的特​​定区域进行的骨骼样品中,发现单位质量的焓值相对于骨骼古代而言呈指数下降。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号