TY - JOUR
T1 - Revisiting ligation at selenomethionine
T2 - Insights into native chemical ligation at selenocysteine and homoselenocysteine
AU - Dardashti, Rebecca Notis
AU - Metanis, Norman
N1 - Publisher Copyright:
© 2017 Elsevier Ltd
PY - 2017
Y1 - 2017
N2 - 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.
AB - 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.
KW - Chemical protein synthesis
KW - Native chemical ligation
KW - Peptide methylation
KW - Selenocysteine
KW - Selenomethionine
UR - http://www.scopus.com/inward/record.url?scp=85020114535&partnerID=8YFLogxK
U2 - 10.1016/j.bmc.2017.05.006
DO - 10.1016/j.bmc.2017.05.006
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C2 - 28526476
AN - SCOPUS:85020114535
SN - 0968-0896
VL - 25
SP - 4983
EP - 4989
JO - Bioorganic and Medicinal Chemistry
JF - Bioorganic and Medicinal Chemistry
IS - 18
ER -