Rapid nickel(ii)-promoted cysteine: S -arylation with arylboronic acids

Kengo Hanaya; Jun Ohata; Mary K. Miller; Alicia E. Mangubat-Medina; Michael J. Swierczynski; David C. Yang; Reece M. Rosenthal; Brian V. Popp; Zachary T. Ball

doi:10.1039/c9cc00159j

Rapid nickel(ii)-promoted cysteine: S -arylation with arylboronic acids

Kengo Hanaya, Jun Ohata, Mary K. Miller, Alicia E. Mangubat-Medina, Michael J. Swierczynski, David C. Yang, Reece M. Rosenthal, Brian V. Popp, Zachary T. Ball

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

36 Citations (Scopus)

Abstract

S-Arylation of cysteine residues is an increasingly powerful tool for site-specific modification of proteins, providing novel structure and electronic perturbation. The present work demonstrates an operationally-simple cysteine arylation reaction 2-nitro-substituted arylboronic acids, promoted by a simple nickel(ii) salt. The process exhibits strikingly fast reaction rates under physiological conditions in purely aqueous media with excellent selectivity toward cysteine residues. Cysteine arylation of natural proteins and peptides allows attachment of useful reactive handles for stapling, imaging, or further conjugation.

Original language	English
Pages (from-to)	2841-2844
Number of pages	4
Journal	Chemical Communications
Volume	55
Issue number	19
DOIs	https://doi.org/10.1039/c9cc00159j
Publication status	Published - 2019
Externally published	Yes

ASJC Scopus subject areas

Catalysis
Electronic, Optical and Magnetic Materials
Ceramics and Composites
Chemistry(all)
Surfaces, Coatings and Films
Metals and Alloys
Materials Chemistry

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10.1039/c9cc00159j

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title = "Rapid nickel(ii)-promoted cysteine: S -arylation with arylboronic acids",

abstract = "S-Arylation of cysteine residues is an increasingly powerful tool for site-specific modification of proteins, providing novel structure and electronic perturbation. The present work demonstrates an operationally-simple cysteine arylation reaction 2-nitro-substituted arylboronic acids, promoted by a simple nickel(ii) salt. The process exhibits strikingly fast reaction rates under physiological conditions in purely aqueous media with excellent selectivity toward cysteine residues. Cysteine arylation of natural proteins and peptides allows attachment of useful reactive handles for stapling, imaging, or further conjugation.",

author = "Kengo Hanaya and Jun Ohata and Miller, {Mary K.} and Mangubat-Medina, {Alicia E.} and Swierczynski, {Michael J.} and Yang, {David C.} and Rosenthal, {Reece M.} and Popp, {Brian V.} and Ball, {Zachary T.}",

note = "Funding Information: We acknowledge support from the Robert A. Welch Foundation Research Grant C-1680 (Z. T. B.), from the National Science Foundation under grant number CHE-1055569 (Z. T. B.). We thank Chenfei Yu and Han Xiao for protein expression efforts and advice. Publisher Copyright: {\textcopyright} 2019 The Royal Society of Chemistry.",

year = "2019",

doi = "10.1039/c9cc00159j",

language = "English",

volume = "55",

pages = "2841--2844",

journal = "Chemical Communications",

issn = "1359-7345",

publisher = "Royal Society of Chemistry",

number = "19",

}

TY - JOUR

T1 - Rapid nickel(ii)-promoted cysteine

T2 - S -arylation with arylboronic acids

AU - Hanaya, Kengo

AU - Ohata, Jun

AU - Miller, Mary K.

AU - Mangubat-Medina, Alicia E.

AU - Swierczynski, Michael J.

AU - Yang, David C.

AU - Rosenthal, Reece M.

AU - Popp, Brian V.

AU - Ball, Zachary T.

N1 - Funding Information: We acknowledge support from the Robert A. Welch Foundation Research Grant C-1680 (Z. T. B.), from the National Science Foundation under grant number CHE-1055569 (Z. T. B.). We thank Chenfei Yu and Han Xiao for protein expression efforts and advice. Publisher Copyright: © 2019 The Royal Society of Chemistry.

PY - 2019

Y1 - 2019

N2 - S-Arylation of cysteine residues is an increasingly powerful tool for site-specific modification of proteins, providing novel structure and electronic perturbation. The present work demonstrates an operationally-simple cysteine arylation reaction 2-nitro-substituted arylboronic acids, promoted by a simple nickel(ii) salt. The process exhibits strikingly fast reaction rates under physiological conditions in purely aqueous media with excellent selectivity toward cysteine residues. Cysteine arylation of natural proteins and peptides allows attachment of useful reactive handles for stapling, imaging, or further conjugation.

AB - S-Arylation of cysteine residues is an increasingly powerful tool for site-specific modification of proteins, providing novel structure and electronic perturbation. The present work demonstrates an operationally-simple cysteine arylation reaction 2-nitro-substituted arylboronic acids, promoted by a simple nickel(ii) salt. The process exhibits strikingly fast reaction rates under physiological conditions in purely aqueous media with excellent selectivity toward cysteine residues. Cysteine arylation of natural proteins and peptides allows attachment of useful reactive handles for stapling, imaging, or further conjugation.

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VL - 55

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EP - 2844

JO - Chemical Communications

JF - Chemical Communications

IS - 19

ER -

Rapid nickel(ii)-promoted cysteine: S -arylation with arylboronic acids

Abstract

ASJC Scopus subject areas

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