Self-Assembly of Elastin-like Polypeptide Brushes on Silica Surfaces and Nanoparticles

Control over the placement and activity of biomolecules on solid surfaces is a key challenge in bionanotechnology. While covalent approaches excel in performance, physical attachment approaches excel in ease of processing, which is equally important in many applications. We show how the precision of recombinant protein engineering can be harnessed to design and produce protein-based diblock polymers with a silica-binding and highly hydrophilic elastin-like domain that self-assembles on silica surfaces and nanopartides to form stable polypeptide brushes that can be used as a scaffold for later biofunctionalization. From atomic force microscopy-based single-molecule force spectroscopy, we find that individual silica-binding peptides have high unbinding rates. Nevertheless, from quartz crystal microbalance measurements, we find that the self-assembled polypeptide brushes cannot easily be rinsed off. From atomic force microscopy imaging and bulk dynamic light scattering, we find that the binding to silica induces fibrillar self-assembly of the peptides. Hence, we conclude that the unexpected stability of these self-assembled polypeptide brushes is at least in part due to peptide-peptide interactions of the silica-binding blocks at the silica surface.

Automated summary

Control over biomolecule placement and activity on solid surfaces is crucial in bionanotechnology. Recombinant protein engineering can be used to design protein-based diblock polymers that self-assemble on silica surfaces and form stable polypeptide brushes for biofunctionalization. The stability of these brushes is partly due to peptide-peptide interactions at the silica surface, as evidenced by high unbinding rates of silica-binding peptides and fibrillar self-assembly induced by silica binding.