On the bulk biomechanical behavior of densely cross-linked dentin matrix: The role of induced-glycation, regional dentin sites and chemical inhibitor.
On the bulk biomechanical behavior of densely cross-linked dentin matrix: The role of induced-glycation, regional dentin sites and chemical inhibitor.
复制标题
关于密集交联牙本质基质的整体生物力学行为：诱导糖化、区域牙本质位点和化学抑制剂的作用。
DOI：
10.1016/j.jmbbm.2019.103589
复制
发表时间：
2020
影响因子：
3.9
通讯作者：
Bedran-Russo,AnaK
中科院分区：
文献类型：
--
作者：
Alania,Yvette;Trevelin,LiviaT;Hussain,Mohammad;Zamperini,CamilaA;Mustafa,Gresa;Bedran-Russo,AnaK
Collagen glycation takes place under physiological conditions during chronological aging, leading to the formation of advanced glycation end-products (AGEs). AGEs accumulation induces non-enzymatic collagen cross-links increasing tissue stiffness and impairing function. Here, we focused on determining the cumulative effect of induced glycation on the mechanical behavior of highly collagen cross-linked dentin matrices and assess the topical inhibition potential of aminoguanidine. Bulk mechanical characterization suggests that early glycation cross-links significantly increase the tensile strength and stiffness of the dentin matrix and promote a brittle failure response. Histologically, glycation yielded a more mature type I collagen in a densely packed collagen matrix. The time-dependent effect of glycation indicates cumulative damage of dentin matrices that is partially inhibited by aminoguanidine. The regional dentin sites were differently affected by induced-glycation, revealing the crown dentin to be mechanically more affected by the glycation protocol. These findings in human dentin set the foundation for the proposed in vitro ribose-induced glycation model, which produces an early matrix stiffening mechanism by reducing tissue viscoelasticity and can be partially inhibited by topical aminoguanidine.
