Protein folding is a dynamic process of molecular self-assembly during which a single stranded polypeptide chain folds to form a well-defined, three-dimensional tertiary structure that exhibits a function. Inspired by nature’s way, we explored several approaches to prepare synthetic analogues of folded proteins. The single-chain folding of synthetic polymers bearing self-assembling motifs is here evaluated in water. Benzene-1,3,5-tricarboxamides (BTAs) were applied as the recognition motif to induce single chain folding under selected conditions. Remarkably, increasing the chain length results in cylindrically shaped nano-objects in which the length increases with increasing degree of polymerization, while the cross-section remains constant. The addition of catalytic sites provides the SCPNs with a function. For example, embedding a catalytically active site in the interior of the SCPNs affords efficient catalysis in water.The precise location of self-assembling motifs within the polymer chain and the position of the catalytically active unit appear to be of crucial importance to improve the functioning of SCPNs. As a result, enhanced control over polydispersities and sequence control are an important next step to make in the field of functional SCPNs. Recent advances in sequence controlled polymerizations and precision polymerizations will undoubtedly provide novel opportunities to achieve this challenge

Controlling function through structure in dynamic single chain polymeric nanoparticles

254th National Meeting (2017)

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