Synthesis of peptides with α,β-dehydroamino acids, VI. Synthesis ofN-benzyloxycarbonyl andN-trifluoroacetyl dipeptides of α,β-dehydro-butyrine, -valine, -leucine, and -isoleucine

Condensation of Z- and TFA-amino acid amides with 2-oxo-acids, namely butanoic, 3-methylbutanoic, 4-methylpentanoic, and (3RS)-3-methylpentanoic acid, yields (in the presence of p-toluenesulfonic acid as a catalyst) Z- and TFA-dipeptides with C-terminal ΔAbu2) (1–4), ΔVal (5–8), ΔLeu (9–11), and ΔIle (12–15) (Table 1).

LOWER ALIPHATIC 2-OXOACIDS AND THEIR ETEYL ESTERS FROM ETHYL ESTERS OF 2-HYDROXY ACIDS

(1989). LOWER ALIPHATIC 2-OXOACIDS AND THEIR ETEYL ESTERS FROM ETHYL ESTERS OF 2-HYDROXY ACIDS. Organic Preparations and Procedures International: Vol. 21, No. 1, pp. 75-82.

Coordination of copper(II) ions by α,β-dehydro-dipeptides. Potentiometric and spectroscopic study

Abstract Potentiometric and spectroscopic data have shown that the double bond within dehydro-peptides considerably affects their behaviour as ligands relative to their saturated parents, with proton and copper(II) ions.

Co-ordination of copper(II) ions by prolyl-α,β-dehydroamino acids: comparative studies and general considerations

Potentiometric and spectroscopic measurements and theoretical calculations have revealed that α,β-dehydroamino acid residues have a considerable effect on the co-ordination ability of an adjacent amide nitrogen towards Cu2+ ions. Also the side chain of such residues affects the stability constants and, in some cases, the binding mode of short peptides containing α,β-dehydroamino acid residues. The theoretical calculations showed that all dehydroamino acids except α,β-dehydroalanine tend to bend a peptide chain towards a turn conformation. This has a very strong impact on the co-ordination ability of a dehydropeptide ligand.

Unusual binding ability of α,β-dehydrodipeptides towards metal ions

Abstract Ni II , Zn II and Co II complexes of α,β-dehydro-dipeptides (containing Gly, Leu, Ala, Val or Phe residues) were studied by potentiometric and spectroscopic methods. Deprotonation and coordination of amide nitrogens occurred in all cases around the physiological pH range. The dipeptides with composition of Xaa-Δ-Ala formed octahedral species, while Gly-Δ-Xaa (Xaa = Leu or Phe) formed square planar bis complexes with Ni II .

Conformational investigation of α,β-dehydropeptides VII*. Conformation of Ac-Pro-ΔAla-NHCH3 and Ac-Pro-(E)-ΔAbu-NHCH3: comparison with (Z)-substituted α,β-dehydropeptides†

The crystal structure and solution conformation of Ac-Pro-deltaAla-NHCH3 and the solution conformation of Ac-Pro-(E)-deltaAbu-NHCH3 were investigated by X-ray diffraction method and NMR, FTIR and CD spectroscopies. Ac-Pro-deltaAla-NHCH3 adopts an extended-coil conformation in the crystalline state, with all-trans peptide bonds and the deltaAla residue being in a C5 form, phi(1)=-71.4(4), psi(1)=-16.8(4), phi(2)= -178.4(3) and psi(2)= 172.4(3) degrees. In inert solvents the peptide also assumes the C5 conformation, but a gamma-turn on the Pro residue cannot be ruled out. In these solvents Ac-Pro-(E)-deltaAbu-NHCH3 accommodates a beta(II)-turn, but a minor conformer with a nearly planar dispo…

N-Acetyl-α, β-dehydroamino acid N’-methylamides and N’, N’-Dimethylamides

Conformational investigation of αβ-dehydropeptides

Solution conformations of three series of model peptides, homochiral Ac-Pro-L-Xaa-NHCH3 and heterochiral Ac-Pro-D-Xaa-NHCH3 (Xaa = Val, Phe, Leu, Abu, Ala) as well as alpha,beta-unsaturated Ac-Pro-delta Xaa-NHCH3 [delta Xaa = delta Val, (Z)-delta Phe, (Z)-delta Leu, (Z)-delta Abu] were investigated in CDCl3 and CH2Cl2 by 1H-, 13C-NMR, and FTIR spectroscopy. NH stretching absorption spectra, solvent shifts delta delta for NH (Xaa) and NHCH3 on going from CDCl3 to (CD3)2SO, diagnostic interresidue proton NOEs, and trans-cis isomer ratios were examined. These studies performed showed the essential difference in conformational propensities between homochiral peptides (L-Xaa) on the one hand and…