Computationally designed peptides for self-assembly of nanostructured lattices.

ABSTRACT: Folded peptides present complex exterior surfaces specified by their amino acid sequences, and the control of these surfaces offers high-precision routes to self-assembling materials. The complexity of peptide structure and the subtlety of noncovalent interactions make the design of predetermined nanostructures difficult. Computational methods can facilitate this design and are used here to determine 29-residue peptides that form tetrahelical bundles that, in turn, serve as building blocks for lattice-forming materials. Four distinct assemblies were engineered. Peptide bundle exterior amino acids were designed in the context of three different interbundle lattices in addition to one design to produce bundles isolated in solution. Solution assembly produced three different types of lattice-

SUBMITTER: Zhang HV 

PROVIDER: S-EPMC5017825 | biostudies-literature | 2016 Sep

REPOSITORIES: biostudies-literature