119767-96-3

Upstream product

• 10065-72-2 L-Alanine methyl ester 
• 97521-30-7 N-carboxy Boc-Leu-ΔPhe anhydride 
• 13139-15-6 N-tert-butoxycarbonyl-L-leucine 
• 193069-45-3 Boc-Leu-ΔLeu-Leu-OMe 
• 193069-44-2 Boc-Leu-ΔLeu-Val-OMe 
• 193069-43-1 Boc-Leu-ΔLeu-Gly-OMe 
• 108450-83-5 Boc-L-Leu-(Z)-ΔLeu*NCA 
• 108460-59-9 Boc-L-Leu-(Z)-ΔLeu-L-Ala-OMe 
• 74805-42-8 N-carboxy-α-dehydrophenylalanine anhydride 
• 83791-32-6 N-carboxy dehydrophenylalanine anhydride 
• 7625-53-8 D-alanine methyl ester 
• 117187-08-3 Boc-Leu-ΔPhe-NCA 

Downstream Products

• 123975-76-8 Boc-L-Leu-D-Phe-L-Ala-OMe 
• 123975-76-8 Boc-L-Leu-L-Phe-L-Ala-OMe 

Relevant academic research and scientific papers

Dehydrooligopeptides. XX. Unusual Peptide Bond Cleavage of Dehydrotripeptide Esters Containing α-Dehydroamino Acid Residue at P2 by Using Papain

Enzymatic ester hydrolysis and coupling of various N- protected Δ2 - dehydrotripeptide methyl esters (Boc-AA-ΔAA-AA-OMe) (4) by using protease papain in Mcllvaine buffer are mainly described. The substrates (4) used were prepared by one-pot coupling of N-carboxy-α-dehydroamino acid anhydride (ΔAA·NCA) with N- and C-component L-α-amino acids (AA). Even in the enzymatic reaction of 4 containing an unusual ΔAA residue, the normal ester hydrolysis took place to give Boc-AA-ΔAA-AA-OH (6) and, in certain cases, the interesting unusual peptide bond cleavage at P2 of 6 occured further to give the unexpected N-(1,2-dioxoalkyl)-AA-OH. Besides examining in detail the differences between the enzymatic actions to the structures of 4, we also studied the mechanisms of the ester and peptide bond hydrolyses. As the results, the reverse enzymatic coupling of 4 with H-AA-ΔVal-OMe was first achieved to give dehydropentapeptide containing two ΔAA residues.

Correlation between the Configurational Structure and the Asymmetric Hydrogenation of Δ1-, Δ2-, and Δ3-Dehydrotripeptides

The heterogeneous catalytic hydrogenation of Δ1-dehydrotripeptides (Δ1-DHP), which have a β-turn structure, was carried out to give the corresponding tripeptides indicative of the very large diastereomeric excess, comparing with thos

Syntheses and Separations of Diastereomers of Protected-Δ1-, Δ2-, and Δ3-Dehydrotripeptides

Total eighteen kinds of Δ1-, Δ2-, and Δ3-dehydrotripeptides (DHP) containing of a ΔPhe and two chiral α-amino acid residues were synthesized and the diastereomeric mixture of DHP were subjected to the HPLC separation.From the results and the 1H NMR spectral data, it was found to be significant relationship between the separation and the conformational structure of DHP.