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Luis Moroder1, Hans-Jürgen Musiol1

  • 1Bioorganic Chemistry, Max-Planck Institute of Biochemistry, Martinsried, Germany.

Journal of Peptide Science : an Official Publication of the European Peptide Society
|December 20, 2019
PubMed
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Chalcogen amino acids like methionine, selenomethionine, and telluromethionine are incorporated into proteins. Researchers use these natural and synthetic compounds to study protein structure and function.

Area of Science:

  • Biochemistry
  • Chemical Biology
  • Structural Biology

Background:

  • Chalcogen elements (oxygen, sulfur, selenium) are vital in natural amino acids.
  • Heavier chalcogens like tellurium lack discovered functions.
  • Methionine, selenomethionine, and telluromethionine are incorporated into proteins.

Purpose of the Study:

  • To review the incorporation and application of chalcogen amino acids in protein research.
  • To explore the use of synthetic chalcogen-containing amino acid analogues.

Main Methods:

  • Analysis of proteinogenic amino acids and their chalcogen analogues.
  • Investigation of tRNA synthetase tolerance for non-canonical amino acids.
  • Application of synthetic peptides and recombinant DNA (rDNA) expressed proteins.
Keywords:
methoxininepeptidesproteinsredox potentialsselenocysteine and tellurocysteineselenomethionine and telluromethionineβ-(thienopyrrolyl)- and β-(selenolopyrrolyl)-alanineβ-selenienylalanine and β-tellurienylalanineβ-thienylalanine

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Main Results:

  • Selenomethionine and telluromethionine are incorporated into proteins, likely due to tRNA synthetase tolerance.
  • Synthetic analogues like thiophene, selenophene, and tellurophene can be incorporated into proteins.
  • Selenocysteine is a proteinogenic amino acid inserted via a special translation mechanism.

Conclusions:

  • Chalcogen amino acids, both natural and synthetic, offer unique physicochemical properties.
  • These properties are valuable for modulating structure and function in peptides and proteins.
  • Further research utilizes these compounds to advance peptide and protein studies.