In recent decades, chemical protein synthesis and the development of chemoselective reactions—including ligation reactions—have led to significant breakthroughs in protein science. Among them are a better understanding of protein structure-function relationships, the study of protein posttranslational modifications, exploration of protein design, unnatural amino acid incorporation, and the study of therapeutic proteins and protein folding. Chalcogen chemistry, especially that of sulfur and selenium, is quite rich, and we have witnessed continuous progress in this field in recent years. In this short review, we will instead summarize three stories that we have recently presented on chalcogen chemistry and its impact on protein science, which was presented in the Miklós Bodanszky Award Lecture at the 35th European Peptide Society Meeting in Dublin, Ireland, 26 August 2018.
Bibliographical noteFunding Information:
N.M. acknowledges the Israel Science Foundation (783/18), the German-Israeli Foundation for Scientific Research and Development (GIF) (I-1355-302.5/2016), and Israel Cancer Research Fund for financial support. R.N.D. and O.W.K. thank the Kaete Klausner Fellowship and R.M. thanks the Maydan Fellowship.
© 2019 European Peptide Society and John Wiley & Sons, Ltd.
- chemical protein synthesis
- methylene thioacetal
- oxidative folding