Catechol and amine residues, both abundantly present in mussel adhesion proteins, are known to act cooperatively by displacing hydration barriers before binding to mineral surfaces. In spite of synthetic efforts toward mussel-inspired adhesives, the effect of positioning of the involved functional groups along a polymer chain is not well understood. By using sequence-defined oligomers grafted to soft hydrogel particles as adhesion probes, we study the effect of catechol–amine spacing, as well as positioning relative to the oligomer terminus. We demonstrate that the catechol–amine spacing has a significant effect on adhesion, while shifting their position has a small effect. Notably, combinations of non-charged amides and catechols can achieve similar cooperative effects on adhesion when compared to amine and catechol residues. Thus, these findings provide a blueprint for the design of next generation mussel-inspired adhesives.

中文翻译：

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胺和酰胺残基的序列定义定位，以控制邻苯二酚驱动的湿粘附

已知贻贝粘附蛋白中大量存在的儿茶酚和胺残基在结合矿物质表面之前通过取代水合屏障来协同作用。尽管人们对贻贝类胶粘剂进行了综合性努力，但对沿聚合物链定位的相关官能团的定位效果尚不甚了解。通过使用嫁接到软水凝胶颗粒上的序列定义的低聚物作为粘附探针，我们研究了邻苯二酚-胺间距以及相对于低聚物末端的定位的影响。我们证明，邻苯二酚-胺的间距对附着力有显着影响，而移动其位置则影响很小。值得注意的是，当与胺和邻苯二酚残基相比时，不带电荷的酰胺和邻苯二酚的组合可以在粘附上实现类似的协同作用。从而，