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Peer-reviewedCC BYRSC chemical biology

Bromo-desthiobiotin (Br-DTB) tag for unbiased profiling and identification of chemical modifications.

  • Bibhuti Bhusana Palai1
  • Daniel H Ramirez1
  • Changfeng Deng2
  • Francisca N de Luna Vitorino1
  • Chenfeng Zhao2
  • Dong Zhu3,4
  • Dongwen Lv3,4
  • Benjamin A Garcia1
  • Zongtao Lin2
4 affiliations
  1. 1Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine in St. Louis MO 63110 USA [email protected].
  2. 2Department of Medicinal Chemistry, Rutgers University Piscataway NJ 08854 USA [email protected].
  3. 3Department of Cellular Biology and Anatomy, Medical College of Georgia, Augusta University Augusta Georgia 30912 USA.
  4. 4Georgia Cancer Center, Augusta University Augusta Georgia 30912 USA.
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Abstract

Leveraging the intrinsic reactivity of cysteine, isoTOP-ABPP (activity-based protein profiling) has been a powerful chemoproteomic platform for cysteine quantification, ligand, and chemical modification discovery. Here, we report new bromo-desthiobiotin azide (Br-DTB) tags for covalent labelling, enabling unbiased identification of chemical modifications. Besides peptide identification from MS2 spectra, Br's isotopic MS1 signatures provide an additional layer of validation to confirm labelled sites and eliminate false-positive assignments. To support this analysis, we have developed a publicly available in-house software to automatically recognize this isotopic signature. The accuracy of the Br-DTB tag was further validated by a synthetic peptide in vitro and l-azidohomoalanine (AHA) labelling in living cells. We further elucidated the covalent labelling site of piperlongumine (PL) on the E3 ligase KEAP1, demonstrating its utility for discovering new covalent labelling sites. Collectively, Br-DTB tags are suitable for chemoproteomic workflows, providing a robust platform for covalent labelling discovery and functional proteome profiling.

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Cite

BibTeXRIS
BibTeX
@article{palai2026bromodesthiobiotin,
  title = {{Bromo-desthiobiotin (Br-DTB) tag for unbiased profiling and identification of chemical modifications.}},
  author = {Bibhuti Bhusana Palai and Daniel H Ramirez and Changfeng Deng and Francisca N de Luna Vitorino and Chenfeng Zhao and Dong Zhu and Dongwen Lv and Benjamin A Garcia and Zongtao Lin},
  journal = {RSC chemical biology},
  year = {2026},
  month = oct,
  doi = {10.1039/d6cb00192k},
  url = {https://europepmc.org/article/MED/42903947},
  note = {CC BY},
}
RIS
TY  - JOUR
TI  - Bromo-desthiobiotin (Br-DTB) tag for unbiased profiling and identification of chemical modifications.
AU  - Bibhuti Bhusana Palai
AU  - Daniel H Ramirez
AU  - Changfeng Deng
AU  - Francisca N de Luna Vitorino
AU  - Chenfeng Zhao
AU  - Dong Zhu
AU  - Dongwen Lv
AU  - Benjamin A Garcia
AU  - Zongtao Lin
PY  - 2026
DA  - 2026/10/14
JO  - RSC chemical biology
DO  - 10.1039/d6cb00192k
UR  - https://europepmc.org/article/MED/42903947
AB  - Leveraging the intrinsic reactivity of cysteine, isoTOP-ABPP (activity-based protein profiling) has been a powerful chemoproteomic platform for cysteine quantification, ligand, and chemical modification discovery. Here, we report new bromo-desthiobiotin azide (Br-DTB) tags for covalent labelling, enabling unbiased identification of chemical modifications. Besides peptide identification from MS2 spectra, Br's isotopic MS1 signatures provide an additional layer of validation to confirm labelled sites and eliminate false-positive assignments. To support this analysis, we have developed a publicly available in-house software to automatically recognize this isotopic signature. The accuracy of the Br-DTB tag was further validated by a synthetic peptide in vitro and l-azidohomoalanine (AHA) labelling in living cells. We further elucidated the covalent labelling site of piperlongumine (PL) on the E3 ligase KEAP1, demonstrating its utility for discovering new covalent labelling sites. Collectively, Br-DTB tags are suitable for chemoproteomic workflows, providing a robust platform for covalent labelling discovery and functional proteome profiling.
SN  - 2633-0679
ER  -