Crystal structure of N-(tert-but-oxy-carbon-yl)phenyl-alanylde-hydro-alanine isopropyl ester (Boc-Phe-ΔAla-OiPr)

Acta Crystallogr Sect E Struct Rep Online. 2014 Nov 29;70(Pt 12):599-602. doi: 10.1107/S1600536814025197. eCollection 2014 Dec 1.

Abstract

In the title compound, the de-hydro-dipeptide (Boc-Phe-ΔAla-OiPr, C20H28N2O5), the mol-ecule has a trans conformation of the N-methyl-amide group. The geometry of the de-hydro-alanine moiety is to some extent different from those usually found in simple peptides, indicating conjugation between the H2C=C group and the peptide bond. The bond angles around de-hydro-alanine have unusually high values due to the steric hindrance, the same inter-action influencing the slight distortion from planarity of the de-hydro-alanine. The mol-ecule is stabilized by intra-molecular inter-actions between the isopropyl group and the N atoms of the peptide main chain. In the crystal, an N-H⋯O hydrogen bond links the mol-ecules into ribbons, giving a herringbone head-to-head packing arrangement extending along the [100] direction. In the stacks, the mol-ecules are linked by weak C-H⋯O hydrogen-bonding associations.

Keywords: crystal structure; de­hydro peptides; de­hydro­alanine; herringbone packing; α,β-de­hydro­amino acids.