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The α-Hydrazino-Peptide 8-Helix: A Key Role for Homochiral Hydrazino Turns
David J Aitken1, Valérie Declerck1
1Université Paris-Saclay, CNRS, ICMMO, 17 avenue des Sciences, 91400 Orsay, France.
None:
8-Helix secondary structures have rarely been described in peptidomimetic foldamers. By combining the propensity of α-hydrazino acids to form hydrazino turns (i.e., stabilized C8 conformations) with the conformational restrictions induced by a four-membered ring, homooligomers of the cyclic α-hydrazino acid (R)-N-aminoazetidine-2-carboxylic acid (AAzC) adopt robust 8-helix architectures. These folded structures display contiguous homochiral hydrazino turns with an S configuration at each sp3 nitrogen.
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