Abstract
A hydrogen‐bonding interface between helical aromatic oligoamide foldamers has been designed to promote the folding of a helix‐turn‐helix motif with a head‐to‐tail arrangement of two helices of opposite handedness. This design complements an earlier helix‐turn‐helix motif with a head‐to‐head arrangement of two helices of identical handedness interface. The two motifs were shown to have comparable stability and were combined in a unimolecular tetra‐helix fold constituting the largest abiotic tertiary structure to date.
Highlights
A hydrogen-bonding interface between helical aromatic oligoamide foldamers has been designed to promote the folding of a helix-turn-helix motif with a head-to-tail arrangement of two helices of opposite handedness
The design of tertiary folds is a considerable challenge. This challenge is worth pursuing because tertiary folding is the level at which sophisticated functions emerge in proteins and the same may be expected for foldamers
The way is being paved by impressive progress in protein design[2] and increasing mastery in programming binding interfaces between peptidic structures, in particular within peptide helix bundles.[2b,c,3] For instance, helix bundles have been reported in peptidomimetics, such as b-peptides[4] and b-ureas.[5]
Summary
A hydrogen-bonding interface between helical aromatic oligoamide foldamers has been designed to promote the folding of a helix-turn-helix motif with a head-to-tail arrangement of two helices of opposite handedness. Hydrogen-bonding patterns involving X (a) and Y (b) units.
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