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Methods and Applications of Expressed Protein Ligation

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Expressed Protein Ligation

Part of the book series: Methods in Molecular Biology ((MIMB,volume 2133))

Abstract

Expressed protein ligation is a method of protein semisynthesis and typically involves the reaction of recombinant protein C-terminal thioesters with N-cysteine containing synthetic peptides in a chemoselective ligation. The recombinant protein C-terminal thioesters are produced by exploiting the action of nature’s inteins which are protein modules that catalyze protein splicing. This chapter discusses the basic principles of expressed protein ligation and recent advances and applications in this protein semisynthesis field. Comparative strengths and weaknesses of the method and future challenges are highlighted.

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Acknowledgments

We thank the NIH (GM62437 and CA74305) and the Leukemia and Lymphoma Society for financial support. We are grateful to Cole lab members, past and present, for their intellectual and experimental efforts that contributed to some of the work described here.

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Authors and Affiliations

  1. Division of Genetics, Department of Medicine, Brigham and Women’s Hospital, Harvard Medical School, Boston, MA, USA

    Zhipeng A. Wang & Philip A. Cole

  2. Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA, USA

    Zhipeng A. Wang & Philip A. Cole

Authors
  1. Zhipeng A. Wang
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  2. Philip A. Cole
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Correspondence to Philip A. Cole .

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Editors and Affiliations

  1. ProteoDesign, Barcelona, Barcelona, Spain

    Miquel Vila-Perelló

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Wang, Z.A., Cole, P.A. (2020). Methods and Applications of Expressed Protein Ligation. In: Vila-Perelló, M. (eds) Expressed Protein Ligation. Methods in Molecular Biology, vol 2133. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-0434-2_1

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  • DOI: https://doi.org/10.1007/978-1-0716-0434-2_1

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  • Publisher Name: Humana, New York, NY

  • Print ISBN: 978-1-0716-0433-5

  • Online ISBN: 978-1-0716-0434-2

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