Evidence for the 3 10 ‐helical structure of peptides based on antAib, a fluorophoric, anthracene‐fused, 1‐aminocyclopentane‐1‐carboxylic acid

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   i α →C   i αcyclized, C α,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/3 10 ‐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 biopolymers@wiley.com