Foldamer Tertiary Structure through Sequence-Guided Protein Backbone Alteration.

ABSTRACT: The prospect of recreating the complex structural hierarchy of protein folding in synthetic oligomers with backbones that are artificial in covalent structure ("foldamers") has long fascinated chemists. Foldamers offer complex functions from biostable scaffolds and have found widespread applications in fields from biomedical to materials science. Most precedent has focused on isolated secondary structures or their assemblies. In considering the goal of complex protein-like tertiary folding patterns, a key barrier became apparent. How does one design a backbone with covalent connectivity and a sequence of side-chain functional groups that will support defined intramolecular packing of multiple artificial secondary structures? Two developments were key to overcoming this challenge. First was

SUBMITTER: George KL 

PROVIDER: S-EPMC5953838 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature