Title of article
Cyclopropane analogue of valine: influence of side chain orientation on peptide folding
Author/Authors
Jiménez، نويسنده , , Ana I. and Marraud، نويسنده , , Michel and Cativiela، نويسنده , , Carlos، نويسنده ,
Issue Information
هفته نامه با شماره پیاپی سال 2003
Pages
4
From page
3147
To page
3150
Abstract
The cyclopropane analogue of valine (1-amino-2,2-dimethylcyclopropanecarboxylic acid, c3Val) has been synthesised and incorporated into the model peptides tBuCO-l-Pro-l-c3Val-NHiPr and tBuCO-l-Pro-d-c3Val-NHiPr. In the solid state, both dipeptides accommodate a type II β-turn stabilised by an NHiPr to tBuCO hydrogen bond. Remarkably, the peptide incorporating l-c3Val also exhibits a distorted γ-turn around the cyclopropane residue, with Pro-CO and NHiPr intramolecularly hydrogen-bonded.
Keywords
2 , 3-methanovaline , cyclopropane amino acid , X-ray diffraction , peptide conformation , crystal structure , peptide structure , beta-turn , gamma-turn , constrained amino acid , peptide turn
Journal title
Tetrahedron Letters
Serial Year
2003
Journal title
Tetrahedron Letters
Record number
1661679
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