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Preferred conformation of peptides rich in alicyclic C α,α ‐disubstituted glycines
Author(s) -
Toniolo C.,
Crisma M.,
Formaggio F.,
Benedetti E.,
Santini A.,
Iacovino R.,
Saviano M.,
Di Blasio B.,
Pedone C.,
Kamphuis J.
Publication year - 1996
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/(sici)1097-0282(1996)40:5<519::aid-bip9>3.0.co;2-z
Subject(s) - alicyclic compound , chemistry , amino acid , stereochemistry , fourier transform infrared spectroscopy , aminoisobutyric acid , organic chemistry , biochemistry , chemical engineering , engineering
The conformational preferences of the alicyclic C α,α ‐disubstituted glycines Ac n c (1‐amino‐1‐cycloalkane‐carboxylic acid; n = 4, 7, 9, 12) were assessed in selected model compounds, including homopeptides and Ala (or Aib, α‐aminoisobutyric acid)/Ac n c peptides containing a small total number of residues, by Fourier transform ir absorption, 1 H‐nmr, and x‐ray diffraction analyses. The results obtained indicate that β‐turn and 3 10 ‐helical structures are preferentially adopted by short peptides rich in these cycloaliphatic α‐amino acids. © 1997 John Wiley & Sons, Inc. Biopoly 40: 519–522, 1996