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Preferred conformation of peptides rich in alicyclic Cα,α-disubstituted glycines

✍ Scribed by C. Toniolo; M. Crisma; F. Formaggio; E. Benedetti; A. Santini; R. Iacovino; M. Saviano; B. Di Blasio; C. Pedone; J. Kamphuis

Publisher
Wiley (John Wiley & Sons)
Year
1996
Tongue
English
Weight
245 KB
Volume
40
Category
Article
ISSN
0006-3525

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✦ Synopsis

The conformational preferences of the alicyclic C","-disubstituted glycines Ac,c (I-amino-I-cycloalkane-carboxylic acid; n = 4 , 7, 9, 1 2 ) were assessed in selected model compounds, including homopeptides and Ala (or Aib, a-aminoisobutyric acid)lAc,c peptides containing a small total number of residues, by Fourier transform ir absorption, 'H-nmr, and x-ray diffraction analyses. The results obtained indicate that p-turn and 310-helical structures are preferentially adopted by short peptides rich in these cycloaliphatic a-amino acids.

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