Structural Investigation of “cis” and “trans” Vinylogous Peptides:  cis-Vinylog Turn in Folded cis-Vinylogous Peptides, an Excellent Mimic of the Natural β-Turn - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Journal of Organic Chemistry Année : 2005

Structural Investigation of “cis” and “trans” Vinylogous Peptides:  cis-Vinylog Turn in Folded cis-Vinylogous Peptides, an Excellent Mimic of the Natural β-Turn

Résumé

Various sequences of modified peptides including those containing a cis- or trans-vinylogous residue have been studied using X-ray diffraction in the solid state and 1H NMR and IR spectroscopy in solution. A cis-vinylogous residue promotes an NH to CO intramolecular H-bond, closing a nine-membered pseudocycle that stabilizes a folded moiety that we proposed to name the cis-vinylogous turn. A trans-vinylogous residue involves an extended conformation. Two consecutive vinylogous residues retain their own structural propensity:  “Xaatr”-“Xaacis” or “Xaacis”-“Xaatr” sequence is singly folded, whereas “Xaacis”-“Xaacis” sequence is doubly folded. Oligo vinylogs with all-trans or all-cis or alternating cis−trans motifs could constitute new classes of foldamers

Domaines

Chimie

Dates et versions

hal-00022581 , version 1 (11-04-2006)

Identifiants

Citer

Claude Grison, Philippe Coutrot, Stéphane Genève, C. Didierjean, Michel Marraud. Structural Investigation of “cis” and “trans” Vinylogous Peptides:  cis-Vinylog Turn in Folded cis-Vinylogous Peptides, an Excellent Mimic of the Natural β-Turn. Journal of Organic Chemistry, 2005, 70 (26), pp.10753-10764. ⟨10.1021/jo051483y⟩. ⟨hal-00022581⟩
44 Consultations
1 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More