Selenomethionine (Sem) has been incorporated recombinantly into proteins many times to elucidate their structure and function. In this paper, we revisit incorporation via chemical protein synthesis to shed light on the mechanism of native chemical ligation. The effect of chalcogen position on ligation is investigated, and selenium-containing peptide ligation is optimized. Additionally, selective methylation is performed on selenolates in a peptide in the presence of unprotected thiols.
Bibliographical noteFunding Information:
This work was supported by Israel Science Foundation (1072/14), the US-Israel Binational Science Foundation (BSF) (2014167), and the German-Israeli Foundation for Scientific Research and Development (GIF) (I-1355-302.5/2016). R.N.D. thanks the Kaete Klausner Fellowship for financial support. We thank Orit Ktorza and Reem Mousa for their support, Israel Alshanski for NMR assistance, and Dr. Post Sai Reddy for assistance in homoselenocystine synthesis.
© 2017 Elsevier Ltd
- Chemical protein synthesis
- Native chemical ligation
- Peptide methylation