Thermolysin-catalyzed synthesis of peptide amides.

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Abstract
Enzymatic condensation by thermolysin between various amino acid amides and N.alpha.-protected or unprotected peptides was examined. As models, three protected tetrapeptide amides, Boc-Trp-Met-Asp-X, Boc-Ser-Glu-Ala-X and Boc-Ser-Lys-Ala-X, and two unprotected tetrapeptide amides, H-Trp-Met-Asp-X and H-Phe-Met-Arg-X, were prepared [X = Phe-NH2, Leu-NH2, Phe-NHEt, Val-NH2, Ala-NH2, (p-fluoro)Phe-NH2], and the effects of various experimental conditions (pH, solvent and time) were examined. In addition, the C-terminal of oxidized insulin B-chain was elongated to an amide by addition of various amides mentioned above with the aid of thermolysin.