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Applied Microbiology and Biotechnology

, Volume 73, Issue 4, pp 740–754 | Cite as

In vivo engineering of proteins with nitrogen-containing tryptophan analogs

  • Sandra Lepthien
  • Birgit Wiltschi
  • Bojana Bolic
  • Nediljko BudisaEmail author
Mini-Review

Abstract

Recently, it has become possible to reprogram the protein synthesis machinery such that numerous noncanonical amino acids can be translated into target sequences yielding tailor-made proteins. The canonical amino acid tryptophan (Trp) encoded by a single nucleotide triplet (UGG) is a particularly interesting target for protein engineering and design. Trp-residues can be substituted with a variety of analogs and surrogates generated biosynthetically or by organic chemistry. Among them, nitrogen-containing tryptophan analogs occupy a central position, as they have distinct chemical properties in comparison with aliphatic amines and imines. They resemble purine bases of DNA and share their capacity for pH-sensitive intramolecular charge transfer. These special properties of the analogs can be directly transmitted into related protein structures via in vivo ribosome-mediated translation. Proteins expressed in this way are further endowed with unique properties like new spectral, altered redox and titration features or might serve as useful biomaterials. We present and discuss current works and future developments in protein engineering with nitrogen-containing tryptophan analogs and related compounds as well as their relevance for academic and applicative research.

Keywords

Amino- and azatryptophan Genetic code Nucleobase fluorescence Protein design and engineering DNA mimicry 

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Copyright information

© Springer-Verlag 2006

Authors and Affiliations

  • Sandra Lepthien
    • 1
  • Birgit Wiltschi
    • 1
  • Bojana Bolic
    • 1
  • Nediljko Budisa
    • 1
    Email author
  1. 1.Molecular BiotechnologyMax-Planck-Institut für Biochemie, BioFuture Independent Research GroupMartinsriedGermany

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