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

ABSTRACT: 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 nanoparticles 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 cryst

SUBMITTER: Alvisi N 

PROVIDER: S-EPMC8154268 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature