We demonstrate spatially selective nucleation of peptide nanostructures, subsequent hydrogel self-assembly, and control of material properties, by exploiting immobilized enzymes on both flat synthetic surfaces and magnetic nanoparticles (NPs) for the localized catalytic production of oligopeptide hydrogelators. This is inspired by the observation that biological systems often regulate self-assembly by coupling to enzyme catalyzed formation or breakdown of molecular building blocks. A combination of transmission electron microscopy (TEM), high pressure liquid chromatography, circular dichroism spectroscopy, and rheological characterization shows that thin nanofibrous meshes can be prepared on flat surfaces and that hydrogels with increased mechanical strength can be obtained. The magnetic NPs may further be manipulated to control the timing of gelation. TEM shows that the NPs in the gelled structures formed organizational nodes from which a high-density of nanofibers emanated. The NPs are tightly integrated in the hydrogel structure and enable a "magnetic hydrogel". The self-assembled surface and NP-based nanostructures are reminiscent of those observed naturally in a cellular context and may have potential applications in biocatalysis, tissue engineering, controlled release, and drug delivery.

Localized peptide self-assembly on nanoparticles and surfaces

2019 Spring National Meeting

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