Search results for "dehydroalanine"
showing 6 items of 26 documents
Synthesis of dehydrodipeptide esters and their evaluation as inhibitors of cathepsin C
2015
The procedures for the synthesis of esters of dehydropeptides containing C-terminal (Z)-dehydrophenylalanine and dehydroalanine have been elaborated. These esters appeared to be moderate or weak inhibitors of cathepsin C, with some of them exhibiting slow-binding behavior. As shown by molecular modeling, they are rather bound at the surface of the enzyme and are not submersed in its binding cavities. Electronic supplementary material The online version of this article (doi:10.1007/s00044-015-1366-0) contains supplementary material, which is available to authorized users.
Synthesis of peptides with α,β‐dehydroamino acids, III. Debenzyloxycarbonylation and detrifluoroacetylation of dehydroalanine and dehydrophenylalanin…
1985
The removal of amino protecting groups from a series of twelve model Z-3) or TFA-dipeptides of dehydroalanine and (Z)-dehydrophenylalanine was investigated. During this deprotection, peptides with Δ Ala are prone to side reactions to a higher extent than those with Δ Phe. Therefore it is interesting to note that from the Δ Ala peptides, the Z group can be split off in preparative manner with HCO2NH4 in the presence of Pd C (Table 4). Synthese von Peptiden mit α,β-Dehydroaminosauren, III.– Debenzyloxycarbonylierung und Detrifluoracetylierung von Dehydroalanin- und Dehydrophenylalanin-Peptiden An einer Serie von zwolf Z-3) oder TFA-Modellpeptiden mit Dehydroalanin und (Z)-Dehydrophenylalanin …
Conformational studies of hexapeptides containing two dehydroamino acid residues in positions 3 and 5 in peptide chain
2008
Abstract Synthesis and structural studies of hexapeptides containing two dehydroamino acid residues in positions 3 and 5 in a peptide chain were performed. All the investigated peptides adopted bent conformations, stabilized by intramolecular hydrogen bonding, and could exist as two different conformers in solution. Only in the case of the peptide containing ΔAla residues, expected 3 10 -helical conformation was found.
Conformation of dehydropentapeptides containing four achiral amino acid residues - controlling the role of L-valine.
2014
Structural studies of pentapeptides containing an achiral block, built from two dehydroamino acid residues (ΔZPhe and ΔAla) and two glycines, as well as one chiral L-Val residue were performed using NMR spectroscopy. The key role of the L-Val residue in the generation of the secondary structure of peptides is discussed. The obtained results suggest that the strongest influence on the conformation of peptides arises from a valine residue inserted at the C-terminal position. The most ordered conformation was found for peptide Boc-Gly-ΔAla-Gly-ΔZPhe-Val-OMe (3), which adopts a right-handed helical conformation.
Synthesis of Peptides with α,β-Dehydroamino Acids, II. Synthesis oftert-Butyloxycarbonyldipeptides of Dehydroalanine and Dehydrophenylalanine
1985
Condensation of amides of Boc-amino acids3) with pyruvic acid leads to Boc-dipeptides 1 – 3 of dehydroalanine and 1-Boc-5-alkyl-2-methyl-4-oxo-2-imidazolidinecarboxylic acids 8 – 10. The amides, however, do not condense with phenylpyruvic acid. Boc-dipeptides of dehydroalanine (1 – 3) and dehydrophenylalanine (4 – 7) are synthesized using (Boc)2O and dehydrodipeptides with a free unmasked N-terminal amino group. Synthese von Peptiden mit α,β-Dehydroaminosauren, II1). – Synthese von tert-Butyloxycarbonyldipeptiden von Dehydroalanin und Dehydrophenylalanin2) Die Kondensation von Boc-Aminosaureamiden3) mit Brenztraubensaure fuhrt zu Boc-Dipeptiden 1 – 3 des Dehydroalanins und 1-Boc-5-alkyl-2-m…
Crystal structure ofN-(tert-butoxycarbonyl)glycyl-(Z)-β-bromodehydroalanine methyl ester [Boc–Gly–(β-Br)(Z)ΔAla–OMe]
2014
In a dehydroamino acid with a C=C bond between the α- and β-C atoms, the amino acid residues are linked trans to each other and there are no strong intramolecular hydrogen bonds. The torsion angles indicate a non-helical conformation of the molecule.