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Evidence for the 3 10 ‐helical structure of peptides based on antAib, a fluorophoric, anthracene‐fused, 1‐aminocyclopentane‐1‐carboxylic acid
Author(s) -
Wright Karen,
Lohier JeanFrançois,
Wakselman Michel,
Mazaleyrat JeanPaul,
Peggion Cristina,
Formaggio Fernando,
Toniolo Claudio
Publication year - 2007
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.20841
Subject(s) - random hexamer , chemistry , anthracene , fluorescence , preprint , carboxylic acid , absorption (acoustics) , amino acid , stereochemistry , combinatorial chemistry , organic chemistry , crystallography , biochemistry , materials science , physics , quantum mechanics , world wide web , computer science , composite material
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