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Synthesis 2002(6): 0726-0732
DOI: 10.1055/s-2002-25762
PAPER
© Georg Thieme Verlag Stuttgart · New York

Synthesis of a Precursor of Bioactive Pentapeptide OGP-(10-14) and the Fragment of Enkephalin Catalyzed by MCM-22 Immobilized or Free Proteases in Organic Solvents

Ping Liua, Yun-hua Ye*a, Gui-ling Tiana, Kin-Sing Leeb, Man-Sau Wongb, Wai-hung Lob
a The Key Laboratory of Bioorganic Chemistry and Molecular Engineering, Ministry of Education, Department of Chemistry, Peking University, Beijing, 100871, PRC
b Open Laboratory of Chirotechnology and Department of Applied Biology and Chemical Technology, The Hong Kong Polytechnic University, Kowloon, Hong Kong, PRC
Fax: +86(10)62751708; e-Mail: yhye@pku.edu.cn;
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Publication History

Received 16 January 2002
Publication Date:
26 April 2002 (online)

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Abstract

Full enzymatic synthesis of a precursor of osteogenic growth peptide fragment (10-14), Z-Tyr-Gly-Phe-Gly-Gly-OEt, was accomplished using immobilized proteases on molecular sieve MCM-22 by adsorption as catalyst via 3+2 synthetic route for the first time. The reuse time of immobilized enzyme was dependent on concrete reaction system. Compared with free enzyme, the reaction rate catalyzed by immobilized enzyme was remarkably enhanced and its synthetic yield was also increased in most cases. The effects of water content and the added amount of Et3N on synthesis of fragments of bioactive peptides including OGP-(10-14) and enkephalin by immobilized enzymes were different from free enzyme.

Key words

immobilized enzyme - MCM-22 - OGP-(10-14) - enzymatic peptide synthesis - organic solvents

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The IUPAC-IUB Joint Commission on Biochemical Nomenclature (JCBN), Eur. J. Biochem. 1984, 138, 9.