ArticleChemistry, an Asian journal2026
Binol as a Bioisosteres for Hairpin and Parallel β-pleated Sheet Mimetic Foldamer.
Article in Chemistry, an Asian journal, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
In this study, the efficient design and synthesis of a novel peptide bioisosteres for selective folding into a hairpin-like structure has been reported. The peptide mimetic comprises β-alanine, L-leucine, α-amino isobutyric acid, m-nitro cinnamic acid has been synthesized via solution-phase coupling methods. A hairpin conformation and extended β-pleated parallel sheet assembly have been characterized in solution as well as in solid state. The key to this success was the use of β-alanine as a flexible amino acid that can accommodate a wide range of dihedral angles proximal to the binol core. In its solid state, the molecule adopts a hairpin conformation with two perpendicular naphthalene rings. The centrally located binol segment act as bioisosteres and nucleates a chain reversal in the hairpin conformation. Two intramolecular cross-strand hydrogen bonds stabilize the hairpin. Moreover, the intermolecular NH…O═C hydrogen bonds connect the hairpins into an infinitely extended parallel β-sheet. The structure is also stabilized by face to edge π-stacking interactions. This peptide bioisosteres represents a promising tool for foldamer design.
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