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.
MeSH terms
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Antimony / chemistry*
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Arsenic / chemistry*
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Bismuth / chemistry*
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Cysteine / chemistry
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Humans
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Lanthanoid Series Elements / chemistry
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Luminescent Measurements / methods
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Models, Molecular
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Nuclear Magnetic Resonance, Biomolecular / methods*
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Peptide Hydrolases / analysis*
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Sulfhydryl Compounds / chemistry
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Zika Virus / enzymology*
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Zika Virus Infection / virology
Substances
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Lanthanoid Series Elements
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Sulfhydryl Compounds
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Antimony
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Peptide Hydrolases
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Cysteine
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Arsenic
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Bismuth