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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
Contributor : Julie Gonnet <>
Submitted on : Tuesday, January 7, 2020 - 1:55:51 PM
Last modification on : Tuesday, October 13, 2020 - 10:45:54 AM

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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, American Chemical Society, 2020, ⟨10.1021/acs.joc.9b02916⟩. ⟨hal-02430577⟩

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