Supramolecular polymerization of proteinaceous or synthetic macromolecules often proceeds slowly due to the long nucleation stage in the self-assembly process. In nature, actin polymerization can be regulated by nucleation factors (e.g. Arp2/3 complex), which dramatically accelerate the nucleation and growth of actin filaments for temporal controls over critical biological functions. Many of these nucleation factors act as scaffolds to increase the local concentration and interaction of monomers for accelerated nucleation. Inspired by this mechanism, we studied the accelerated supramolecular polymerization of synthetic polypeptides (PLGs) into amyloid fibrils by introducing silica nanoparticles (NPs) as artificial nucleation factors, demonstrating the role of complementary electrostatic interaction that plays in the binding and assembly process. From the kinetics experiments and model-based analysis, we propose that the NP-nucleated PLG assembly follows a generalized heterogeneous nucleation pathway, with the kinetic rates coupled to the binding affinity of monomers on the nucleation factors. This approach might be applicable for acceleration and regulation of supramolecular polymerization of charged macromolecules in general and for development of nanostructured materials by controlled supramolecular polymerization.

Regulating the supramolecular polymerization of synthetic polypeptides by artificial nucleation factors

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.