Direct Editing of Cysteine to Electrophilic Alkyl Halides in Peptides

Functional group conversion is a cornerstone of modern synthetic chemistry. Many strategies routinely employed for small-molecule transformations are unsuitable for modifying biomacromolecules, including peptides. Here, we describe a simple but chemoselective approach that directly converts the nucleophilic cysteine carbon-thiol side chain into an electrophilic carbon-halogen bond under mild conditions, compatible with diverse peptides. The incorporation of this versatile synthetic handle facilitates a range of subsequent transformations that are rarely, if ever, applied to complicated peptides. We envision that this side-chain editing methodology will open a broad expanse of unexplored peptide chemical space, which will concomitantly unlock applications for an entire class of new biomacromolecules.

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Publication Details

Journal
Journal of the American Chemical Society
Published
2025-08-05
DOI
https://doi.org/10.1021/jacs.5c06200
Citations
2
Primary Topic
Click Chemistry and Applications
Type
article
Field-Weighted Citation Impact
1.87

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article

Direct Editing of Cysteine to Electrophilic Alkyl Halides in Peptides

H. Greenberg, Jacob M. Goldberg, Daniel S. Honeycutt, Fang Wang et al.
2 citations
Journal of the American Chemical Society
Click Chemistry and Applications
1.87
article

Direct Editing of Cysteine to Electrophilic Alkyl Halides in Peptides

H. Greenberg, Jacob M. Goldberg, Daniel S. Honeycutt, Fang Wang, W. H. McCarthy, Jason M. Mrosla, Brian Pallares, Waldo Salgado-Bello
article en
2 citations

Abstract

Functional group conversion is a cornerstone of modern synthetic chemistry. Many strategies routinely employed for small-molecule transformations are unsuitable for modifying biomacromolecules, including peptides. Here, we describe a simple but chemoselective approach that directly converts the nucleophilic cysteine carbon-thiol side chain into an electrophilic carbon-halogen bond under mild conditions, compatible with diverse peptides. The incorporation of this versatile synthetic handle facilitates a range of subsequent transformations that are rarely, if ever, applied to complicated peptides. We envision that this side-chain editing methodology will open a broad expanse of unexplored peptide chemical space, which will concomitantly unlock applications for an entire class of new biomacromolecules.

Journal of the American Chemical SocietyVol. 147(32)
University of Rhode Island (US), Colgate University (US)
National Science Foundation, National Institute of General Medical Sciences
Openalex Percentile: Top 14%
Click Chemistry and Applications
1.87
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Direct Editing of Cysteine to Electrophilic Alkyl Halides in Peptides — H. Greenberg, Jacob M. Goldberg, et al. · Journal of the American Chemical Society (2025) | TGRS Research Map | TGRS