Subtilisin and α-chymotrypsin catalyzed synthesis of peptides containing arginine and lysine p-nitroanilides as c-terminal moieties
✍ Scribed by Valentin M. Stepanov; Elena Yu. Terent'eva; Tatiana L. Voyushina; Mikhail Yu. Gololobov
- Book ID
- 103992121
- Publisher
- Elsevier Science
- Year
- 1995
- Tongue
- English
- Weight
- 612 KB
- Volume
- 3
- Category
- Article
- ISSN
- 0968-0896
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✦ Synopsis
Almtract---p-Nitroanilides of N-acylated di-, tri-and tetrapeptides with C-terminal arginine or lysine residues have been obtained, as a rule with good yields, via acylation of arginine or lysine p-nitroanilides by methyl esters of respective N-acylated peptides, catalyzed by subtilisin or ct-ehymotrypsin. The synthesis might be performed by two routes---by reaction in waterorganic solvent mixtures, catalyzed by dissolved enzyme, or by condensation of the components in organic solvents with low water content in the presence of any enzyme distributed over a silica support surface. The second approach seems to be preferable due to suppression of hydrolytic side reactions and improved stability of an enzyme. Subtilisin 72 is especially effective as a catalyst for the acylation of p-nitroanilides by N-protected tripeptide methyl esters---the derivatives capable of occupying the S t, S 2 and S 3 subsites of its extended binding site. Even dipeptide esters with D-amino acids in P2 position can be applied for p-nitroanilide acylation. The efficiency of ¢z-chymotrypsin as a catalyst for peptide synthesis is more limited due to restricted specificity of this enzyme.