Collect. Czech. Chem. Commun. 1985, 50, 2775-2782

Enzymatically catalyzed synthesis of oxytocin fragments 1-6 and 7-9

Václav Čeřovský and Karel Jošt

Institute of Organic Chemistry and Biochemistry, Czechoslovak Academy of Sciences, 166 10 Prague 6


Papain, α-chymotrypsin, thermolysin and elastase were utilized in the synthesis of peptide bonds of the protected oxytocin nonapeptide, except the S-benzylcysteine-proline bond. Amino groups were protected with benzyloxycarbonyl or tert-butyloxycarbonyl groups, carboxy groups as ethyl ester, phenylhydrazides or amides. The cysteine sulfhydryl group was blocked with the benzyl group whereas the tyrosine hydroxyl was unprotected. Most of the fragments were synthesized in satisfactory yields using an equimolar ratio of both reaction components and minimal (experimentally determined) amount of the given enzyme.