Biological Soft Matter Group, Department of Living Matter, AMOLF, 1098 XG Amsterdam, The Netherlands.
Physical Chemistry and Soft Matter, Wageningen University and Research, 6708 WE Wageningen, The Netherlands.
Proc Natl Acad Sci U S A. 2020 Apr 14;117(15):8326-8334. doi: 10.1073/pnas.1920062117. Epub 2020 Apr 1.
Collagen forms the structural scaffold of connective tissues in all mammals. Tissues are remarkably resistant against mechanical deformations because collagen molecules hierarchically self-assemble in fibrous networks that stiffen with increasing strain. Nevertheless, collagen networks do fracture when tissues are overloaded or subject to pathological conditions such as aneurysms. Prior studies of the role of collagen in tissue fracture have mainly focused on tendons, which contain highly aligned bundles of collagen. By contrast, little is known about fracture of the orientationally more disordered collagen networks present in many other tissues such as skin and cartilage. Here, we combine shear rheology of reconstituted collagen networks with computer simulations to investigate the primary determinants of fracture in disordered collagen networks. We show that the fracture strain is controlled by the coordination number of the network junctions, with less connected networks fracturing at larger strains. The hierarchical structure of collagen fine-tunes the fracture strain by providing structural plasticity at the network and fiber level. Our findings imply that low connectivity and plasticity provide protective mechanisms against network fracture that can optimize the strength of biological tissues.
胶原蛋白构成了所有哺乳动物结缔组织的结构支架。由于胶原蛋白分子在纤维网络中分层自组装,使纤维网络随着应变的增加而变硬,因此组织具有很强的抗机械变形能力。然而,当组织受到过度负荷或出现动脉瘤等病理状况时,胶原蛋白网络也会断裂。先前关于胶原蛋白在组织断裂中的作用的研究主要集中在含有高度排列的胶原蛋白束的肌腱上。相比之下,对于在许多其他组织(如皮肤和软骨)中存在的取向更无序的胶原蛋白网络的断裂,人们知之甚少。在这里,我们将重组胶原蛋白网络的剪切流变学与计算机模拟相结合,研究了无序胶原蛋白网络断裂的主要决定因素。我们表明,断裂应变由网络连接点的配位数控制,连接较少的网络在较大应变下断裂。胶原蛋白的层次结构通过在网络和纤维水平上提供结构可塑性来微调断裂应变。我们的研究结果表明,低连接性和可塑性为网络断裂提供了保护机制,这可以优化生物组织的强度。