1. Crystal structure of Boc-(S)-ABOC-(S)-Ala-(S)-ABOC-(S)-Phe-OBn chloro-form monosolvate
- Author
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Emmanuel, Wenger, Laure, Moulat, Baptiste, Legrand, Muriel, Amblard, Monique, Calmès, and Claude, Didierjean
- Subjects
(S)-Phe ,crystal structure ,α,β-hybrid peptide ,11/9 helix ,(S)-1-aminobicyclo[2.2.2]octane-2-carboxylic acid ,OBn ,(S)-ABOC ,Boc ,(S)-Ala ,hydrogen bonding ,Research Communications - Abstract
In the title compound, the α,β-hybrid peptide contains two non-proteinogenic amino acid residues [(S)-ABOC], two amino acid residues [(S)-Ala and (S)-Phe], and protecting groups of Boc and OBn. The tetramer folds into a right-handed mixed 11/9 helix stabilized by intramolecular i,i + 3 and i,i-1 C=O⋯H—N hydrogen bonds. The oligomers are linked into chains by N—H⋯O=C hydrogen bonds with the chloroform solvent molecules intercalated between the folded chains via C—H⋯O=C interactions., In the title compound, phenyl (S)-2-[(S)-(1-{2-[(S)-(1-{[(tert-butoxy)carbonyl]amino}bicyclo[2.2.2]octan-2-yl)formamido]propanamido}bicyclo[2.2.2]octan-2-yl)formamido]-3-phenylpropanoate chloroform monosolvate, C42H56N4O7·CHCl3, the α,β-hybrid peptide contains two non-proteinogenic amino acid residues of (S)-1-aminobicyclo[2.2.2]octane-2-carboxylic acid [(S)-ABOC], two amino acid residues of (S)-2-aminopropanoic acid [(S)-Ala] and (S)-2-amino-3-phenylpropanoic acid [(S)-Phe], and protecting groups of tert-butoxycarbonyl (Boc) and benzyl ester (OBn). The tetramer folds into a right-handed mixed 11/9 helix stabilized by intramolecular i,i + 3 and i,i − 1 C=O⋯H—N hydrogen bonds. In the crystal, the oligomers are linked by N—H⋯O=C hydrogen bonds into chains along the a-axis direction. The chloroform solvent molecules are intercalated between the folded chains via C—H⋯O=C interactions.
- Published
- 2015