Proline as nucleophile in kinetically controlled peptide synthesis catalyze by alcalase in 2-methyl-2-propanol.

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Abstract

Procedures have been developed to synthesize proline-containing peptides in good yields and high purities via a kinetically controlled approach using an industrial alkaline protease, alcalase, as a catalyst in anhydrous 2-methyl-2-propanol. The yield of the reaction was dependent on the structure of the acyl-donor and the water content in the solvent. Using tripeptide as an acyl donor, the yield was higher than that using dipeptide, and when amino acid derivatives were used the yield was the lowest. The yield was also dependent on the concentration of water present in the solvent. The higher the water concentration in the solvent, the lower was the yield in the reaction. Both L-proline or D-proline derivatives could be used as nucleophiles in the reaction.

References (10)

  • M. Philipp et al.

    Molecular & Cellular Biochem.

    (1983)
  • T. Oka et al.

    J. Biochem.

    (1980)
    E. Cheng et al.

    Int. J. Peptide Protein Res.

    (1988)
    J.M. Ricca et al.

    J. Chem. Soc. Perkin Trans. I

    (1989)
  • C.H. Wong et al.

    Experientia

    (1991)
    V. Schellenberger et al.

    Angew Chem. Int. Ed. Engl.

    (1991)
    A.M. Klibanov

    Chemtech.

    (1986)
    L.E.S. Brink et al.

    Enzyme Microb. Technol.

    (1988)
    Y.L. Khmelnitsky et al.

    Enzyme Microb. Technol.

    (1988)
    M.N. Gupta

    Eur. J. Biochem.

    (1992)
    M. Waks

    Proteins: Structure, Function, and Genetics

    (1986)
    J.S. Dordick

    Biotechnol. Prog.

    (1992)
    S.H.M.V. Erp et al.

    Eur. J. Biochem.

    (1991)
  • P. Kuhl et al.

    Tetrahydron Letters

    (1990)
    R. Affleck et al.

    Proc. Natl. Acad. Sci. USA

    (1992)
    H. Kitaguchi et al.

    J. Amer. Chem.

    (1989)
    M. Stahl et al.

    Biotech. Letters

    (1990)
    H. Kise

    Bioorg. Chem.

    (1990)
    H. Kise et al.

    Biotech. Letters

    (1991)
    T. Nagashima et al.

    Enzyme Microb. Technol.

    (1992)
    Z. Zhong et al.

    J. Amer. Chem. Soc.

    (1991)
    C.H. Wong et al.

    J. Amer. Chem. Soc.

    (1990)
    R.S. Phillips et al.

    Enzyme microb. Technol.

    (1990)
    K. Chen et al.

    Biotechnology

    (1991)
There are more references available in the full text version of this article.

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