Peptide tessellation yields micrometre-scale collagen triple helices.
Peptide tessellation yields micrometre-scale collagen triple helices.
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粘性末端的DNA双链体可以自发地结合成长的双螺旋;然而，这种自组装在蛋白质中的发展要少得多。胶原蛋白是细胞外基质中最普遍的成分，也是一种常见的临床生物材料。与天然DNA一样，天然胶原蛋白的103个残基的三螺旋（约300 nm）是化学合成不可接受的。在这里，我们展示了短胶原蛋白模拟肽（CMP）的自组装如何能够制造长度接近一微米的合成胶原蛋白三螺旋。受镶嵌数学的启发，我们推导出设计单CMP的规则，这些CMP自组装成具有完美对称性的长三重螺旋。由此产生的粘性末端在整个组件上是均匀的，并驱动其生长。制定这种设计产生的个人三螺旋匹配或超过那些在天然胶原蛋白的长度和显着的热稳定性，尽管没有高阶协会。CMP的对称组装为开发用于医学和纳米技术的先进材料提供了一个有利的平台。
Sticky-ended DNA duplexes can associate spontaneously into long double helices; however, such self-assembly is much less developed with proteins. Collagen is the most prevalent component of the extracellular matrix and a common clinical biomaterial. Like natural DNA, the ∼103-residue triple-helices (∼300 nm) of natural collagen are recalcitrant to chemical synthesis. Here we show how the self-assembly of short collagen-mimetic peptides (CMPs) can enable the fabrication of synthetic collagen triple-helices that are nearly a micron in length. Inspired by the mathematics of tessellations, we derive rules for the design of single CMPs that self-assemble into long triple helices with perfect symmetry. Sticky-ends thus created are uniform across the assembly and drive its growth. Enacting this design yields individual triple-helices that match or exceed those in natural collagen in length and are remarkably thermostable, despite the absence of higher-order association. Symmetric assembly of CMPs provides an enabling platform for the development of advanced materials for medicine and nanotechnology.