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Modification of Proteases for Peptide Synthesis

  • Jeffrey A. Bibbs (a1), Ziyang Zhong (a1) and Chi-Huey Wong (a1)

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Polypeptides with well defined structures have the potential for the development for novel materials [1]. Synthesis of polypeptides suffer from racemization and protection-deprotection problems and has been dependent on the anhydride method using phosgene. There is definitely a need for a milder, stereoselective, and racemization-free procedure and it appears that enzyme-catalyzed synthesis can provide most of these features. Although proteases have been used in peptide synthesis with the above mentioned advantages, these enzymes have their own inherent catalytic properties which are disadvantageous, that is, they tend to cdeave peptide bonds. Two strategies presented here have been developed to overcome these problems.

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1. Dosch, H.M. and Gelfand, E.W. Methods Enzymol. 150, 223, (1987); L.S. Ramsammy, C. Josepovitz, B.P. Lane and G.J. Kaloyanides, J. Pharmacol. Exp. Ther. 250,149, (1989).
2. Chen, S.T., Hennen, W.J., Bibbs, J.A., Wang, Y.-F., Uu, J.L.-C., and Wong, C.-H. J. Am. Chem. Soc. 112, 945 (1989).
3. Nakagawa, Y. and Mender, M.L. Biochemistry, 9(2), 259, (1970); L.D. Byers and D.E. Koshland, Jr. Bioorganic Chemistry 7, 15, (1978).
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5. Jackson, M.B. and Bender, M.L. Biochem. Biophys. Res. Comm., 39(6), 11571162 (1970).

Modification of Proteases for Peptide Synthesis

  • Jeffrey A. Bibbs (a1), Ziyang Zhong (a1) and Chi-Huey Wong (a1)

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