6s99

Publication Abstract from PubMed

One approach to protein assembly involves water-soluble supramolecular receptors that act like glue. Bionano-architectures directed by these scaffolds are often system-specific with few studies investigating their customization. Here, we describe the modulation of cucurbituril-mediated protein assemblies via the inclusion of peptide tectons. Three peptides of varying length and structural order were N-terminally appended to RSL, a beta-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 consideration of intrinsically disordered peptides (IDPs) as modulatory tectons. Similar to the coiled coil, a mussel adhesion peptide (Mefp) also acted as a spacer between protein-Q7 sheets. In contrast, the fusion of a nucleoporin peptide (Nup) to RSL did not recapitulate the sheet assembly. Instead, a Q -directed cage was adopted, within which disordered Nup peptides were partially "captured" by Q7 receptors. IDP capture occurred by macrocycle recognition of an intrapeptide Phe-Gly motif in which the benzyl side chain was encapsulated by Q7. The modularity of these protein-cucurbituril architectures adds a new dimension to macrocycle-mediated protein assembly. In addition, the segregated crystals, with alternating layers of high and low porosity, provide a basis for new types of materials.

Segregated Protein-Cucurbit[7]uril Crystalline Architectures via Modulatory Peptide Tectons.,Ramberg KO, Guagnini F, Engilberge S, Wronska MA, Rennie ML, Perez J, Crowley PB Chemistry. 2021 Aug 25. doi: 10.1002/chem.202103025. PMID:34432924^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.