Chemical Protein Engineering: Synthetic and Semisynthetic Peptides and Proteins

  • L. Merkel
  • L. Moroder
  • N. Budisa
Part of the Nucleic Acids and Molecular Biology book series (NUCLEIC, volume 22)

Chemical engineering of proteins provides a pool of various synthetic and semisynthetic methods. These involve techniques for the design of peptides and proteins equipped with chemical handles at defined positions in the target structures. Using water-compatible bioorthogonal chemical ligations gained immense importance in chemical and cellular biology for regioselective addressing to target structures. Beside classical protein modifications, we present examples not only of expressed protein modifications, but also of the attachment of small molecules by native and expressed chemical ligation, modified Staudinger ligation, and of the copper(I)-catalyzed Huisgen [3+2] cycloaddition of azides and alkynes. Recently, in addition to enzymatic methods, the use of organometallic chemistry, i.e. regioselective palladium-catalyzed C-C coupling (Sonogashira, Suzuki, and Mizoroki-Heck reactions), became available as a tool for tailored protein modifications. This chapter reviews all traditional and newly developed chemoselective modifications and ligation methods in the field.


Heck Reaction Peptide Bond Formation Protein Splice Native Chemical Ligation LPXTG Motif 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Springer-Verlag Berlin Heidelberg 2009

Authors and Affiliations

  • L. Merkel
    • 1
  • L. Moroder
    • 1
  • N. Budisa
    • 1
  1. 1.Max Planck Institute of BiochemistryGermany

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