Site-selective tagging of proteins by pnictogen-mediated self-assembly

Christoph Nitsche; Mithun C. Mahawaththa; Walter Becker; Thomas Huber; Gottfried Otting

doi:10.1039/c7cc06155b

Site-selective tagging of proteins by pnictogen-mediated self-assembly

Christoph Nitsche^*, Mithun C. Mahawaththa, Walter Becker, Thomas Huber, Gottfried Otting

^*Corresponding author for this work

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

15 Citations (SciVal)

Abstract

Site-selective chemical protein modification is achieved by self-assembly of a specific di-cysteine motif, trivalent pnictogens (As, Sb or Bi) and an aromatic mercaptomethyl-based probe. The strategy is demonstrated with a quaternary complex involving Zika virus protease and a lanthanide ion, enabling paramagnetic nuclear magnetic resonance spectroscopy and luminescence measurements.

Original language	English
Pages (from-to)	10894-10897
Number of pages	4
Journal	Chemical Communications
Volume	53
Issue number	79
DOIs	https://doi.org/10.1039/c7cc06155b
Publication status	Published - 2017

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10.1039/c7cc06155b

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title = "Site-selective tagging of proteins by pnictogen-mediated self-assembly",

abstract = "Site-selective chemical protein modification is achieved by self-assembly of a specific di-cysteine motif, trivalent pnictogens (As, Sb or Bi) and an aromatic mercaptomethyl-based probe. The strategy is demonstrated with a quaternary complex involving Zika virus protease and a lanthanide ion, enabling paramagnetic nuclear magnetic resonance spectroscopy and luminescence measurements.",

author = "Christoph Nitsche and Mahawaththa, \{Mithun C.\} and Walter Becker and Thomas Huber and Gottfried Otting",

note = "Publisher Copyright: {\textcopyright} 2017 The Royal Society of Chemistry.",

year = "2017",

doi = "10.1039/c7cc06155b",

language = "English",

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pages = "10894--10897",

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AU - Nitsche, Christoph

AU - Mahawaththa, Mithun C.

AU - Becker, Walter

AU - Huber, Thomas

AU - Otting, Gottfried

PY - 2017

Y1 - 2017

N2 - Site-selective chemical protein modification is achieved by self-assembly of a specific di-cysteine motif, trivalent pnictogens (As, Sb or Bi) and an aromatic mercaptomethyl-based probe. The strategy is demonstrated with a quaternary complex involving Zika virus protease and a lanthanide ion, enabling paramagnetic nuclear magnetic resonance spectroscopy and luminescence measurements.

AB - Site-selective chemical protein modification is achieved by self-assembly of a specific di-cysteine motif, trivalent pnictogens (As, Sb or Bi) and an aromatic mercaptomethyl-based probe. The strategy is demonstrated with a quaternary complex involving Zika virus protease and a lanthanide ion, enabling paramagnetic nuclear magnetic resonance spectroscopy and luminescence measurements.

UR - http://www.scopus.com/inward/record.url?scp=85030683771&partnerID=8YFLogxK

U2 - 10.1039/c7cc06155b

DO - 10.1039/c7cc06155b

M3 - Article

SN - 1359-7345

VL - 53

SP - 10894

EP - 10897

JO - Chemical Communications

JF - Chemical Communications

IS - 79

ER -

Site-selective tagging of proteins by pnictogen-mediated self-assembly

Abstract

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