Dehydrooligopeptides. XVIII. Enzymatic hydrolysis and coupling of dehydrodipeptide esters containing α-dehydroamino acid residue by using papain

Article abstract of DOI:10.1246/bcsj.68.3549

The enzymatic hydrolysis of N-protected dehydrodipeptide methyl esters (2) (Protect-ΔAA-AA-OMe) was first achieved, despite the requisite of the only neutral and large proteinic L-α-amino acid (AA) in the case using papain. Furthermore, the reverse enzymatic coupling of the C-component 2 with N-component α-amino acid anilides or dehydrodipeptide esters containing dehydrovaline (ΔVal) residue was also successful. Consequently, the present study suggests that the proteolytic enzyme papain is able to become a very useful tool for peptide synthesis by a coupling of the C-component dehydropeptide with N-component α-amino acid, peptide, or dehydropeptide.