A reactive peptide interface for site-selective cysteine bioconjugation
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Updated: Nov 15, 2025
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Synthesis of Protein Bioconjugates via Cysteine-maleimide Chemistry
Published on: July 20, 2016
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Suan Tuang1, Diomedes Dieppa-Matos, Chi Zhang
1Massachusetts Institute of Technology, Department of Chemistry, 77 Massachusetts Avenue, Cambridge, MA 02139, USA.
Chemical Communications (Cambridge, England)
|March 1, 2021
Abstract:
We report aqueous, site-selective modification of proteins using a reactive peptide interface comprising a nine-residue sequence. This interface is the fastest (second-order rate constant of 152 M-1 s-1) catalyst-free, cysteine-based method for modifying proteins available to date, and enables near-quantitative labeling of antibodies in cell lysate.
