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  • Title: Evidence for the 3 10-helical structure of peptides based on antAib, a fluorophoric, anthracene-fused, 1-aminocyclopentane-1-carboxylic acid.
    Author: Wright K, Lohier JF, Wakselman M, Mazaleyrat JP, Peggion C, Formaggio F, Toniolo C.
    Journal: Biopolymers; 2007; 88(6):797-806. PubMed ID: 17803250.
    Abstract:
    Peptides based on 2-amino-2,3-dihydro-1H-cyclopenta[b]anthracene-2-carboxylic acid (antAib), a fluorescent, achiral, alpha-amino acid belonging to the class of C(i) (alpha)-->C(i) (alpha) cyclized, C(alpha,alpha)-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 beta-turns/3(10)-helices. The UV absorption, CD, and fluorescence properties of these antAib/L-Ala model peptides are also described.
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