Revisiting ligation at selenomethionine: Insights into native chemical ligation at selenocysteine and homoselenocysteine

Rebecca Notis Dardashti; Norman Metanis

doi:10.1016/j.bmc.2017.05.006

Revisiting ligation at selenomethionine: Insights into native chemical ligation at selenocysteine and homoselenocysteine

Rebecca Notis Dardashti, Norman Metanis^*

^*Corresponding author for this work

Institute of Chemistry

Research output: Contribution to journal › Article › peer-review

9 Scopus citations

Abstract

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.

Original language	American English
Pages (from-to)	4983-4989
Number of pages	7
Journal	Bioorganic and Medicinal Chemistry
Volume	25
Issue number	18
DOIs	https://doi.org/10.1016/j.bmc.2017.05.006
State	Published - 2017

Bibliographical note

Funding 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.

Publisher Copyright:
© 2017 Elsevier Ltd

Keywords

Chemical protein synthesis
Native chemical ligation
Peptide methylation
Selenocysteine
Selenomethionine

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10.1016/j.bmc.2017.05.006

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title = "Revisiting ligation at selenomethionine: Insights into native chemical ligation at selenocysteine and homoselenocysteine",

abstract = "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.",

keywords = "Chemical protein synthesis, Native chemical ligation, Peptide methylation, Selenocysteine, Selenomethionine",

author = "Dardashti, {Rebecca Notis} and Norman Metanis",

note = "Funding 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. Publisher Copyright: {\textcopyright} 2017 Elsevier Ltd",

year = "2017",

doi = "10.1016/j.bmc.2017.05.006",

language = "American English",

volume = "25",

pages = "4983--4989",

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T1 - Revisiting ligation at selenomethionine

T2 - Insights into native chemical ligation at selenocysteine and homoselenocysteine

AU - Dardashti, Rebecca Notis

AU - Metanis, Norman

N1 - Funding 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. 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

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U2 - 10.1016/j.bmc.2017.05.006

DO - 10.1016/j.bmc.2017.05.006

M3 - Article

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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 -

Revisiting ligation at selenomethionine: Insights into native chemical ligation at selenocysteine and homoselenocysteine

Abstract

Bibliographical note

Keywords

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