Unprecedented Chain‐Length‐Dependent Conformational Conversion Between 11/9 and 18/16 Helix in α/β‐Hybrid Peptides |
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Authors: | Dr. Baptiste Legrand Dr. Christophe André Laure Moulat Emmanuel Wenger Dr. Claude Didierjean Dr. Emmanuel Aubert Dr. Marie Christine Averlant‐Petit Prof. Jean Martinez Dr. Monique Calmes Dr. Muriel Amblard |
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Affiliation: | 1. IBMM, UMR 5247 CNRS, Universités Montpellier 1 et 2, 15 avenue Charles Flahault, 34000 Montpellier (France) http://www.ibmm.univ‐montp1.fr;2. CRM2, UMR 7036 CNRS Université de Lorraine, Boulevard des Aiguilletes, 54506 Vandoeuvre‐lès‐Nancy Cedex (France);3. LCPM—UMR 7568 CNRS Université de Lorraine, 1 rue Grandville, 54001 Nancy Cedex 1 (France) |
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Abstract: | α,β‐Hybrid oligomers of varying lengths with alternating proteogenic α‐amino acid and the rigid β2,3,3‐trisubstituted bicyclic amino acid ABOC residues were studied using both X‐ray crystal and NMR solution structures. While only an 11/9 helix was obtained in the solid state regardless of the length of the oligomers, conformational polymorphism as a chain‐length‐dependent phenomenon was observed in solution. Consistent with DFT calculations, we established that short oligomers adopted an 11/9 helix, whereas an 18/16 helix was favored for longer oligomers in solution. A rapid interconversion between the 11/9 helix and the 18/16 helix occurred for oligomers of intermediate length. |
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Keywords: | 11/9 helix 18/16 helix bicyclic β ‐amino acid foldamers α ,β ‐hybrid peptides |
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