![]() For instance, α-helices and β-sheets are formed and stabilized through H-bonds between backbone carbonyls and N–H groups, where all H-bond donors and acceptors are paired with nearly straight geometry 8, 9. These two unique properties of H-bonding interactions are elegantly utilized in nature to construct the precise three-dimensional structures of nucleic acids and proteins 6, 7. Furthermore, the pattern of H-bond donors and acceptors within molecules capable participating in multiple H-bonds provides specificity by ensuring H-bonding interactions between complementary molecules 5. Compared to other molecular forces including hydrophobic and electrostatic interactions, the alignment of the donor–acceptor pair constituting a H-bond restricts the geometry of the interaction. Hydrogen bonding (H-bonding) interactions are one of the most important non-covalent molecular forces in biology, chemistry, and materials science 1, 2, 3, 4. We further showed the utility of this transition by designing smart, cell-penetrating polymers that undergo acid-activated endosomal escape in living cells. The conformational change of triazole polypeptides in response to the donor-acceptor pattern was conclusively demonstrated using both experimental-based and simulation-based methods. When protonated, the resulting 1,2,3-triazolium ions lose the ability to act as H-bond acceptors, and the polypeptides regain their α-helical structure. Specifically, 1,2,3-triazole groups, when incorporated onto polypeptide side-chains, serve as both H-bond donors and acceptors at neutral pH and disrupt the α-helical conformation. Herein we report a strategy to modulate the conformation of polypeptides utilizing donor–acceptor interactions emanating from side-chain H-bonding ligands. The control over their secondary structures, which enables dynamic conformational changes, is primarily accomplished by tuning the side-chain hydrophobic or ionic interactions. Fig 1 the regions shaded grey mark the putative Δ G b minima.Synthetic polypeptides have received increasing attention due to their ability to form higher ordered structures similar to proteins. The regions associated with peptides’ propensities for the α-helix, C 5 and C 7eq folds are shaded red, yellow and light yellow, respectively, cf. mean FP i of the peptide ligands (Δ G b in kcal mol -1, the width of the FP i averaging window is given in the brackets). Binding affinities Δ G b of the PDZ domains vs.
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