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, 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.
Wright
Karen
K
ILV, UMR CNRS 8180, University of Versailles, F-78035 Versailles, France.
Lohier
Jean-François
JF
Wakselman
Michel
M
Mazaleyrat
Jean-Paul
JP
Peggion
Cristina
C
Formaggio
Fernando
F
Toniolo
Claudio
C
D000409:Alanine / Q000737:chemistry; D000873:Anthracenes / Q000138:chemical synthesis / Q000737:chemistry*; D002942:Circular Dichroism / Q000379:methods; D020650:Combinatorial Chemistry Techniques; D003515:Cycloleucine / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000737:chemistry*; D005453:Fluorescence; D005998:Glycine / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008968:Molecular Conformation; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D017433:Protein Structure, Secondary; D013056:Spectrophotometry, Ultraviolet / Q000379:methods; D017550:Spectroscopy, Fourier Transform Infrared / Q000379:methods