One of the most robust examples of self-assembly in living organisms is the formation of collagen architectures. Collagen type I molecules are a crucial component of the extracellular matrix, where they self-assemble into fibrils of well-defined axial striped patterns. This striped fibrillar pattern is preserved across the animal kingdom and is important for the determination of cell phenotype, cell adhesion, and tissue regulation and signaling. The understanding of the physical processes that determine such a robust morphology of self-assembled collagen fibrils is currently almost completely missing. Here, we develop a minimal coarse-grained computational model to identify the physical principles of the assembly of collagen-mimetic molecules. We find that screened electrostatic interactions can drive the formation of collagen-like filaments of well-defined striped morphologies. The fibril axial pattern is determined solely by the distribution of charges on the molecule and is robust to the changes in protein concentration, monomer rigidity, and environmental conditions. We show that the striped fibrillar pattern cannot be easily predicted from the interactions between two monomers but is an emergent result of multibody interactions. Our results can help address collagen remodeling in diseases and aging and guide the design of collagen scaffolds for biotechnological applications.

中文翻译：

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模拟胶原蛋白分子的原纤维形成

生物体中自组装最有力的例子之一是胶原蛋白结构的形成。I 型胶原蛋白分子是细胞外基质的重要组成部分，在那里它们自组装成具有明确轴向条纹图案的原纤维。这种条纹原纤维图案在整个动物界都保留了下来，对于确定细胞表型、细胞粘附以及组织调节和信号传导很重要。目前几乎完全没有了解决定自组装胶原原纤维如此稳健形态的物理过程。在这里，我们开发了一个最小的粗粒度计算模型来确定胶原蛋白模拟分子组装的物理原理。我们发现筛选的静电相互作用可以驱动形成明确的条纹形态的胶原样细丝。原纤维轴向模式仅由分子上的电荷分布决定，并且对蛋白质浓度、单体刚度和环境条件的变化具有鲁棒性。我们表明，条纹原纤维图案无法从两个单体之间的相互作用中轻易预测，但它是多体相互作用的新兴结果。我们的结果可以帮助解决疾病和衰老中的胶原蛋白重塑问题，并指导用于生物技术应用的胶原蛋白支架的设计。和环境条件。我们表明，条纹原纤维图案无法从两个单体之间的相互作用中轻易预测，但它是多体相互作用的新兴结果。我们的结果可以帮助解决疾病和衰老中的胶原蛋白重塑问题，并指导用于生物技术应用的胶原蛋白支架的设计。和环境条件。我们表明，条纹原纤维图案无法从两个单体之间的相互作用中轻易预测，但它是多体相互作用的新兴结果。我们的结果可以帮助解决疾病和衰老中的胶原蛋白重塑问题，并指导用于生物技术应用的胶原蛋白支架的设计。