Evidence for the 310-helical structure of peptides based on antAib, a fluorophoric, anthracene-fused, 1-aminocyclopentane-1-carboxylic acid

• Published in: Biopolymers 2007, Vol.88 (6), p.797-806
• Main Authors: Wright, Karen, Lohier, Jean-François, Wakselman, Michel, Mazaleyrat, Jean-Paul, Peggion, Cristina, Formaggio, Fernando, Toniolo, Claudio
• Format: Article
• Language: English
• Subjects: 310-helical peptides; antAib; Cα,α‐disubstituted glycine; fluorescent amino acid; α-disubstituted glycine
• ISSN: 0006-3525; 1097-0282
• DOI: 10.1002/bip.20841

Peptides based on 2‐amino‐2,3‐dihydro‐1H‐cyclopenta[b]anthracene‐2‐carboxylic acid (antAib), a fluorescent, achiral, α‐amino acid belonging to the class of C iα→C iα cyclized, Cα,α‐disubstituted glycines, combined with L‐Ala, up to the hexamer level, were synthesized by solution methods and chemically characterized. A conformational analysis by FTIR absorption and NMR techniques suggests that the highest oligomers of this series tend to fold into β‐turns/310‐helices. The UV absorption, CD, and fluorescence properties of these antAib/L‐Ala model peptides are also described. © 2007 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 88: 797–806, 2007. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at [e-mail]