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Modification of Proteases for Peptide Synthesis

Published online by Cambridge University Press:  21 February 2011

Jeffrey A. Bibbs ,
Ziyang Zhong  and
Chi-Huey Wong
Jeffrey A. Bibbs
Affiliation:
Research Institute of Scripps Clinic, Department of Chemistry, La Jolla, CA 92037 and Center for Advanced Materials, Lawrence Berkeley Laboratory, Berkeley, CA 94270
Ziyang Zhong
Affiliation:
Research Institute of Scripps Clinic, Department of Chemistry, La Jolla, CA 92037 and Center for Advanced Materials, Lawrence Berkeley Laboratory, Berkeley, CA 94270
Chi-Huey Wong
Affiliation:
Research Institute of Scripps Clinic, Department of Chemistry, La Jolla, CA 92037 and Center for Advanced Materials, Lawrence Berkeley Laboratory, Berkeley, CA 94270
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Extract

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.

Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 174: Symposium R – Materials Synthesis Utilizing Biological Processes , 1989 , 223
Copyright
Copyright © Materials Research Society 1990

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References

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