Rapid Additive-Free Selenocystine-Selenoester Peptide Ligation

Nicholas J. Mitchell; Lara R. Malins; Xuyu Liu; Robert E. Thompson; Bun Chan; Leo Radom; Richard J. Payne

doi:10.1021/jacs.5b07237

Rapid Additive-Free Selenocystine-Selenoester Peptide Ligation

Nicholas J. Mitchell, Lara R. Malins, Xuyu Liu, Robert E. Thompson, Bun Chan, Leo Radom, Richard J. Payne^*

^*Corresponding author for this work

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

170 Citations (Scopus)

Abstract

We describe an unprecedented reaction between peptide selenoesters and peptide dimers bearing N-terminal selenocystine that proceeds in aqueous buffer to afford native amide bonds without the use of additives. The selenocystine-selenoester ligations are complete in minutes, even at sterically hindered junctions, and can be used in concert with one-pot deselenization chemistry. Various pathways for the transformation are proposed and probed through a combination of experimental and computational studies. Our new reaction manifold is also showcased in the total synthesis of two proteins.

Original language	English
Pages (from-to)	14011-14014
Number of pages	4
Journal	Journal of the American Chemical Society
Volume	137
Issue number	44
DOIs	https://doi.org/10.1021/jacs.5b07237
Publication status	Published - 11 Nov 2015
Externally published	Yes

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10.1021/jacs.5b07237

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title = "Rapid Additive-Free Selenocystine-Selenoester Peptide Ligation",

abstract = "We describe an unprecedented reaction between peptide selenoesters and peptide dimers bearing N-terminal selenocystine that proceeds in aqueous buffer to afford native amide bonds without the use of additives. The selenocystine-selenoester ligations are complete in minutes, even at sterically hindered junctions, and can be used in concert with one-pot deselenization chemistry. Various pathways for the transformation are proposed and probed through a combination of experimental and computational studies. Our new reaction manifold is also showcased in the total synthesis of two proteins.",

author = "Mitchell, {Nicholas J.} and Malins, {Lara R.} and Xuyu Liu and Thompson, {Robert E.} and Bun Chan and Leo Radom and Payne, {Richard J.}",

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AU - Mitchell, Nicholas J.

AU - Malins, Lara R.

AU - Liu, Xuyu

AU - Thompson, Robert E.

AU - Chan, Bun

AU - Radom, Leo

AU - Payne, Richard J.

PY - 2015/11/11

Y1 - 2015/11/11

N2 - We describe an unprecedented reaction between peptide selenoesters and peptide dimers bearing N-terminal selenocystine that proceeds in aqueous buffer to afford native amide bonds without the use of additives. The selenocystine-selenoester ligations are complete in minutes, even at sterically hindered junctions, and can be used in concert with one-pot deselenization chemistry. Various pathways for the transformation are proposed and probed through a combination of experimental and computational studies. Our new reaction manifold is also showcased in the total synthesis of two proteins.

AB - We describe an unprecedented reaction between peptide selenoesters and peptide dimers bearing N-terminal selenocystine that proceeds in aqueous buffer to afford native amide bonds without the use of additives. The selenocystine-selenoester ligations are complete in minutes, even at sterically hindered junctions, and can be used in concert with one-pot deselenization chemistry. Various pathways for the transformation are proposed and probed through a combination of experimental and computational studies. Our new reaction manifold is also showcased in the total synthesis of two proteins.

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U2 - 10.1021/jacs.5b07237

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JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 44

ER -

Rapid Additive-Free Selenocystine-Selenoester Peptide Ligation

Abstract

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