Evidence for the 310-helical structure of peptides based on antAib, a fluorophoric, anthracene-fused, 1-aminocyclopentane-1-carboxylic acid
✍ Scribed by Karen Wright; Jean-François Lohier; Michel Wakselman; Jean-Paul Mazaleyrat; Cristina Peggion; Fernando Formaggio; Claudio Toniolo
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 2007
- Tongue
- English
- Weight
- 212 KB
- Volume
- 88
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
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→C cyclized, 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.
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