Segregated Protein-Cucurbit[7]uril Crystalline Architectures via Modulatory Peptide Tectons.

ABSTRACT: One approach to protein assembly involves water-soluble supramolecular receptors that act like glues. Bionanoarchitectures directed by these scaffolds are often system-specific, with few studies investigating their customization. Herein, the modulation of cucurbituril-mediated protein assemblies through the inclusion of peptide tectons is described. Three peptides of varying length and structural order were N-terminally appended to RSL, a β-propeller building block. Each fusion protein was incorporated into crystalline architectures mediated by cucurbit[7]uril (Q7). A trimeric coiled-coil served as a spacer within a Q7-directed sheet assembly of RSL, giving rise to a layered material of varying porosity. Within the spacer layers, the coiled-coils were dynamic. This result prompted consider

SUBMITTER: Ramberg KO 

PROVIDER: S-EPMC8596587 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature