RESUMEN
α,ß-Dehydroamino acid esters occur in nature. To investigate their conformational properties, a systematic theoretical analysis was performed on the model molecules Ac-ΔXaa-OMe [ΔXaa = ΔAla, (E)-ΔAbu, (Z)-ΔAbu, ΔVal] at the B3LYP/6-311+ + G(d,p) level in the gas phase as well as in chloroform and water solutions with the self-consistent reaction field-polarisable continuum model method. The Fourier transform IR spectra in CCl(4) and CHCl(3) have been analysed as well as the analogous solid state conformations drawn from The Cambridge Structural Database. The ΔAla residue has a considerable tendency to adopt planar conformations C5 (Ï, ψ ≈ - 180°, 180°) and ß2 (Ï, ψ ≈ - 180°, 0°), regardless of the environment. The ΔVal residue prefers the conformation ß2 (Ï, ψ ≈ - 120°, 0°) in a low polar environment, but the conformations α (Ï, ψ ≈ - 55°, 35°) and ß (Ï, ψ ≈ - 55°, 145°) when the polarity increases. The ΔAbu residues reveal intermediate properties, but their conformational dispositions depend on configuration of the side chain of residue: (E)-ΔAbu is similar to ΔAla, whereas (Z)-ΔAbu to ΔVal. Results indicate that the low-energy conformation ß2 is the characteristic feature of dehydroamino acid esters. The studied molecules constitute conformational patterns for dehydroamino acid esters with various side chain substituents in either or both Z and E positions.
Asunto(s)
Aminoácidos/química , Ésteres , Modelos Moleculares , Conformación MolecularRESUMEN
Dehydrobutyrine is the most naturally occurring dehydroamino acid. It is also the simplest dehydroamino acid having the geometrical isomers E/Z. To investigate its conformational properties, a theoretical analysis was performed on N-acetyl-alpha,beta-dehydrobutyrine N'-methylamides, Ac-(E)-DeltaAbu-NHMe and Ac-(Z)-DeltaAbu-NHMe, as well as the dehydrovaline derivative Ac-DeltaVal-NHMe. The phi, psi potential energy surfaces and the localised conformers were calculated at the B3LYP/6-311 + + G(d,p) level of theory both in vacuo and with inclusion of the solvent (chloroform, water) effect (SCRF method). The X-ray crystal structures of Ac-(Z)-DeltaAbu-NHMe and Ac-DeltaVal-NHMe were determined at 85 and 100 K, respectively. The solid-state conformational preferences for the studied residues have been analysed and compared with the other related structures. Despite the limitations imposed by the C(alpha) = C(beta) double bond on the topography of the side chains, the main chains of the studied dehydroamino acids are more flexible than in standard alanine. The studied dehydroamino acids differ in their conformational preferences, which depend on the polarity of the environment. This might be a reason why the nature quite precisely differentiates between DeltaVal and each of the DeltaAbu isomers, and why, particularly so with the latter, they are used as a conformational tool to influence the biological action of usually small, cyclic dehydropeptides.