4.7 Article

Encoding latent SuFEx reactive meta-fluorosulfate tyrosine to expand covalent bonding of proteins

Journal

CHEMICAL COMMUNICATIONS
Volume 58, Issue 48, Pages 6861-6864

Publisher

ROYAL SOC CHEMISTRY
DOI: 10.1039/d2cc01902g

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Funding

  1. NIH [R01CA258300]

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The introduction of new covalent bonds into proteins has provided novel avenues for protein research and applications, but generating covalent linkages remains challenging. In this study, genetically encoded mFSY selectively reacted with specific amino acids, allowing successful engineering of various proteins into covalent binders.
The introduction of new covalent bonds into proteins is affording novel avenues for protein research and applications, yet it remains difficult to generate covalent linkages at all possible sites and across diverse protein classes. Herein, we genetically encoded meta-fluorosulfate-l-tyrosine (mFSY) to selectively react with lysine, tyrosine, and histidine via proximity-enabled SuFEx reaction. mFSY was able to target residues that were elusive for previous unnatural amino acids, and permitted engineering of various proteins including affibody, nanobody, and Fab into covalent binders that irreversibly cross-linked EGFR and HER2. mFSY is thus valuable for developing covalent proteins for biological research, synthetic biology, and biotherapeutics.

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