Peptide and protein have great promise as biomaterials and self-assembled nanostructures. We present a tetrameric peptide scaffold that has been designed to self-assemble into nanostructured lattices and to form unique polymeric structures. Specifically, atomistically resolved structures are reported for three sequences, each sharing a single <i>de novo</i> designed homotetrameric structure comprising four 29-residue peptides and a common scaffold core of hydrophobic amino acid residues. Each structure retains the targeted D2 symmetric (antiparallel) structure. Analysis was performed to compare the crystal structures with the designed structures. In all cases, the designed consensus tetramer core structures were found to have near sub-angstrom RMSD agreement with the resultant crystal structures. Interior residues showed sub-angstrom RMSD agreement, and many exterior sidechain conformations were also found to match closely with the computationally identified side chain conformational states. The tetrameric peptide scaffold provides a robust building unit for the design and study of complex protein nanostructures and presents an exterior surface whose chemistry can be readily modified and programmed.

Atomically resolved structures of computationally designed coiled-coil tetramers used as building blocks for nanostructured lattices and polymers

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.