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Strengthening Peptoid Helicity through Sequence Site-Specific Positioning of Amide Cis-Inducing Nt Bu monomers

Abstract : The synthesis of biomimetic helical secondary structures is sought after for the construction of innovative nanomaterials and applications in medicinal chemistry such as the development of protein-protein interaction modulators. Peptoids, a sequence-defined family of oligomers, enable a peptidomimetic strategy, especially considering the easily accessible monomer diversity and peptoid helical folding propensity. However, cis-trans isomerization of the backbone tertiary amides may impair the peptoid's adoption of stable secondary structures, notably the all-cis polyproline I-like helical conformation. Here, we show that cis-inducing NtBu achiral monomers strategically positioned within chiral sequences may reinforce the degree of peptoid helicity, although with a reduced content of chiral side chains. The design principles presented here will undoubtedly help achieve more conformationally stable helical peptoids with desired functions.
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https://hal.univ-lorraine.fr/hal-02430577
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Submitted on : Thursday, February 3, 2022 - 3:49:09 PM
Last modification on : Wednesday, May 11, 2022 - 4:39:19 AM
Long-term archiving on: : Wednesday, May 4, 2022 - 8:26:53 PM

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Maha Rzeigui, Mounir Traïkia, Laurent Jouffret, Alexandre Kriznik, Jameleddine Khiari, et al.. Strengthening Peptoid Helicity through Sequence Site-Specific Positioning of Amide Cis-Inducing Nt Bu monomers. Journal of Organic Chemistry, 2020, 85 (4), pp.2190-2201. ⟨10.1021/acs.joc.9b02916⟩. ⟨hal-02430577⟩

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