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 (3D) tertiary structure that exhibits a function. Inspired by nature's way, several approaches have been explored to prepare synthetic analogues of folded proteins. We have recently developed single-chain folding of synthetic polymers bearing a single self-assembling motif. Either benzene-1,3,5-tricarboxamides (BTAs) or 2-ureido-4[1H]-pyrimidinones (UPys) were applied as the recognition motif to induce single chain folding under selected conditions. We found that a wide variety of polymer backbones allow the folding of single polymer chains into single chain polymeric nanoparticles (SCPNs). However, the interaction between solvent and recognition motif is crucial to suppress interparticle aggregation. The addition of catalytic sites or fluorescent moieties provides the SCPNs with a function. For example, bipyridine-based SCPNs are effective for sensing Cu(II) at low concentrations while embedding a catalytically active site in the interior of the SCPNs afforded efficient catalysis in water. Precise location of self-assembling motifs within the polymer chain and enhanced control over polydispersities are of crucial importance to improve the scope of SCPNs. Recent advances in sequence controlled polymerizations and precision polymerizations will undoubtedly provide novel opportunities to achieve this.

Folding single polymer chains into single chain polymeric nanoparticles: From structure to function

246th National Meeting (2013)

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