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Herein, the study introduces a novel approach utilizing multifunctional 5\u2010substituted 1,2,3\u2010triazine derivatives to achieve multifaceted bioconjugation targeting cysteine\u2010containing peptides and proteins. On the one hand, this represents an inaugural instance of employing 1,2,3\u2010triazine in biomolecular\u2010specific modification within a physiological solution. On the other hand, as a powerful combination of precision modification and biorthogonality, this strategy allows for the one\u2010pot dual\u2010orthogonal functionalization of biomolecules utilizing the aldehyde group generated simultaneously. 1,2,3\u2010Triazine derivatives with diverse functional groups allow conjugation to peptides or proteins, while bi\u2010triazines enable peptide cyclization and dimerization. The examination of the stability of bi\u2010triazines revealed their potential for reversible peptide modification. This work establishes a comprehensive platform for identifying cysteine\u2010selective modifications, providing new avenues for peptide\u2010based drug development, protein bioconjugation, and chemical biology research.<\/jats:p>","DOI":"10.1002\/advs.202308491","type":"journal-article","created":{"date-parts":[[2024,3,11]],"date-time":"2024-03-11T16:08:45Z","timestamp":1710173325000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":28,"title":["Cysteine\u2010Specific Multifaceted Bioconjugation of Peptides and Proteins Using 5\u2010Substituted 1,2,3\u2010Triazines"],"prefix":"10.1002","volume":"11","author":[{"given":"Quan","family":"Zuo","sequence":"first","affiliation":[{"name":"State Key Laboratory of Bioactive Substance and Function of Natural Medicines Institute of Materia Medica Chinese Academy of Medical Sciences and Peking Union Medical College  Xian Nong Tan Street Beijing 100050 P. R. 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