Morsali Reza, Dai Zhengwei, Wang Yang, Qian Dong, Minary-Jolandan Majid
Department of Mechanical Engineering, The University of Texas at Dallas, 800 W. Campbell Rd, Richardson, Texas 75080, United States.
College of Material and Textile Engineering, Jiaxing University, Jiaxing 314001, China.
ACS Biomater Sci Eng. 2019 Nov 11;5(11):5916-5924. doi: 10.1021/acsbiomaterials.9b00588. Epub 2019 Oct 9.
Noncollagenous proteins at nanoscale interfaces in bone are less than 2-3% of bone content by weight, while they contribute more than 30% to fracture toughness. Major gaps in quantitative understanding of noncollagenous proteins' role in the interfibrillar interfaces, largely because of the limitation of probing their nanoscale dimension, have resulted in ongoing controversies and several outstanding hypotheses on their role and function, arguably going back to centuries ago to the original work from Galileo. Our results from the first detailed computational model of the nano-interface in the bone reveal "synergistic" deformation mechanism of a "double-part" natural glue, that is, noncollagenous osteopontin and osteocalcin at the interfibrillar interface. Specifically, through strong anchoring and formation of dynamic binding sites on mineral nanoplatelets, the nano-interface can sustain a large nonlinear deformation with ductility approaching 5000%. This large deformation results in an outstanding specific energy to failure exceeding ∼350 J/g, which is larger than the most known tough materials (such as Kevlar, spider silk, and so forth.).
骨骼中纳米级界面处的非胶原蛋白按重量计不到骨骼含量的2 - 3%,但其对断裂韧性的贡献超过30%。在定量理解非胶原蛋白在纤维间界面中的作用方面存在重大差距,这主要是由于探测其纳米级尺寸存在局限性,导致了关于其作用和功能的持续争议以及几个突出的假说,这可以追溯到几个世纪前伽利略的原始研究。我们从首个关于骨骼纳米界面的详细计算模型得出的结果揭示了一种“双组分”天然胶水,即纤维间界面处的非胶原蛋白骨桥蛋白和骨钙素的“协同”变形机制。具体而言,通过在矿物纳米片上形成强大的锚固和动态结合位点,纳米界面能够承受大的非线性变形,其延展性接近5000%。这种大变形导致了超过约350 J/g的出色比失效能,这比大多数已知的韧性材料(如凯夫拉尔纤维、蜘蛛丝等)都要大。