In vivo engineering of proteins with nitrogen-containing tryptophan analogs

Sandra Lepthien, Birgit Wiltschi, Bojana Bolic, Nediljko Budisa*

*Corresponding author for this work

Research output: Contribution to journalShort surveypeer-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.

Original languageEnglish
Pages (from-to)740-754
Number of pages15
JournalApplied Microbiology and Biotechnology
Volume73
Issue number4
DOIs
Publication statusPublished - 1 Dec 2006

Keywords

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

ASJC Scopus subject areas

  • Biotechnology
  • Applied Microbiology and Biotechnology

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