Coiled coils 9-to-5: rational <i>de novo</i> design of α-helical barrels with tunable oligomeric states.

ABSTRACT: The rational design of linear peptides that assemble controllably and predictably in water is challenging. Short sequences must encode unique target structures and avoid alternative states. However, the non-covalent forces that stabilize and discriminate between states are weak. Nonetheless, for α-helical coiled-coil assemblies considerable progress has been made in rational de novo design. In these, sequence repeats of nominally hydrophobic (h) and polar (p) residues, hpphppp, direct the assembly of amphipathic helices into dimeric to tetrameric bundles. Expanding this pattern to hpphhph can produce larger α-helical barrels. Here, we show that pentameric to nonameric barrels are accessed by varying the residue at one of the h sites. In peptides wi

SUBMITTER: Dawson WM 

PROVIDER: S-EPMC8503928 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature