Homochiral versus Heterochiral Trifluoromethylated Pseudoproline Containing Dipeptides: A Powerful Tool to Switch the Prolyl-Amide Bond Conformation
In: ISSN: 0022-3263, 2017
Online
academicJournal
Zugriff:
International audience ; The design of constrained peptides is of prime importance in the development of bioactive compounds and for applications in supramolecular chemistry. Due to its nature, the peptide bond undergoes a spontaneous cis–trans isomerism, and the cis isomers are much more difficult to stabilize than the trans forms. By using oxazolidine-based pseudoprolines (ΨPro) substituted by a trifluoromethyl group, we show that the cis peptide bond can be readily switched from 0% to 100% in Xaa-ΨPro dipeptides. Our results prove that changing the configuration of the Cα in Xaa or in ΨPro is sufficient to invert the cis:trans populations while changing the nature of the Xaa side chain finely tuned the conformers ratio. Moreover, a strong correlation is found between the puckering of the oxazolidine ring and the peptide bond conformation. This finding highlights the role of the trifluoromethyl group in the stabilization of the peptide bond geometry. We anticipate that such templates will be very useful to constrain the backbone geometry of longer peptides.
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Homochiral versus Heterochiral Trifluoromethylated Pseudoproline Containing Dipeptides: A Powerful Tool to Switch the Prolyl-Amide Bond Conformation
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Autor/in / Beteiligte Person: | Chaume, Gregory ; Simon, Julien ; Lensen, Nathalie ; Pytkowicz, Julien ; Brigaud, Thierry ; Miclet, Emeric ; Structure et Dynamique des Biomolécules (LBM-E3) ; Laboratoire des biomolécules (LBM UMR 7203) ; Université Pierre et Marie Curie - Paris 6 (UPMC)-Département de Chimie - ENS Paris ; École normale supérieure - Paris (ENS-PSL) ; Université Paris Sciences et Lettres (PSL)-Université Paris Sciences et Lettres (PSL)-École normale supérieure - Paris (ENS-PSL) ; Université Paris Sciences et Lettres (PSL)-Université Paris Sciences et Lettres (PSL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut de Chimie - CNRS Chimie (INC-CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Département de Chimie - ENS Paris ; Université Paris Sciences et Lettres (PSL)-Université Paris Sciences et Lettres (PSL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut de Chimie - CNRS Chimie (INC-CNRS)-Centre National de la Recherche Scientifique (CNRS) ; Laboratoire de Chimie Biologique (LCB) ; Université de Cergy Pontoise (UCP) ; Université Paris-Seine-Université Paris-Seine |
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Zeitschrift: | ISSN: 0022-3263, 2017 |
Veröffentlichung: | HAL CCSD ; American Chemical Society, 2017 |
Medientyp: | academicJournal |
DOI: | 10.1021/acs.joc.7b01944 |
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