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.

胶原蛋白糖基化发生在按时间顺序老化的生理条件下，导致晚期糖基化终产物 (AGEs) 的形成。AGEs 积累诱导非酶胶原交联，增加组织硬度和损害功能。在这里，我们专注于确定诱导糖化对高胶原交联牙本质基质机械行为的累积影响，并评估氨基胍的局部抑制潜力。整体力学表征表明，早期糖化交联显着增加了牙本质基质的拉伸强度和刚度，并促进了脆性破坏反应。组织学上，糖基化在密集的胶原蛋白基质中产生更成熟的 I 型胶原蛋白。糖化的时间依赖性效应表明牙本质基质的累积损伤被氨基胍部分抑制。局部牙本质部位受到诱导糖化的不同影响，表明冠牙本质在机械上更受糖化方案的影响。这些在人类牙本质中的发现为拟议的体外核糖诱导糖基化模型奠定了基础，该模型通过降低组织粘弹性产生早期基质硬化机制，并且可以被局部氨基胍部分抑制。