Unprecedented Chain‐Length‐Dependent Conformational Conversion Between 11/9 and 18/16 Helix in α/β‐Hybrid Peptides1. Issue 48 (26th September 2014)

• Record Type: Journal Article
• Authors: Legrand, Baptiste; André, Christophe; Moulat, Laure; Wenger, Emmanuel; Didierjean, Claude; Aubert, Emmanuel; Averlant‐Petit, Marie Christine; Martinez, Jean; Calmes, Monique; Amblard, Muriel
• Is Part Of: Angewandte Chemie international edition. Volume 53:Issue 48(2014)
• Page Start: 13131
• Page End: 13135
• Publication Date: 2014-09-26
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201407329
• Languages: English
• ISSNs: 1433-7851

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>α, β‐Hybrid oligomers of varying lengths with alternating proteogenic α‐amino acid and the rigid β^{2, 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.</p> </abstract>