ArticleBioconjugate chemistry2017
Targeted Diazotransfer Reagents Enable Selective Modification of Proteins with Azides.
Article in Bioconjugate chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 29 citations in OpenAlex.
- Chemical reactions for the ligand-directed modification of native proteins.Chemical Society reviews · 2026Review
- Progress and challenges in traceless ligand-directed labelling chemistry.Communications chemistry · 2026Review
- Principles and Design of Molecular Tools for Sensing and Perturbing Cell Surface Receptor Activity.Chemical reviews · 2025Review
- Target Bioconjugation of Protein Through Chemical, Molecular Dynamics, and Artificial Intelligence Approaches.Metabolites · 2024Review
- A method for parallel microscale protein labeling and precise control over the average degree of labeling (aDoL).Scientific reports · 2023Article
- Review
- A Strategy to Select Macrocyclic Peptides Featuring Asymmetric Molecular Scaffolds as Cyclization Units by Phage Display.Journal of the American Chemical Society · 2022Article
- Site-selective lysine conjugation methods and applications towards antibody-drug conjugates.Chemical communications (Cambridge, England) · 2021Review
- Iminoboronates as Dual-Purpose Linkers in Chemical Probe Development.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- Bioorthogonal Ligations and Cleavages in Chemical Biology.ChemistryOpen · 2020Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In chemical biology, azides are used to chemically manipulate target structures in a bioorthogonal manner for a plethora of applications ranging from target identification to the synthesis of homogeneously modified protein conjugates. While a variety of methods have been established to introduce the azido group into recombinant proteins, a method that directly converts specific amino groups in endogenous proteins is lacking. Here, we report the first biotin-tethered diazotransfer reagent DtBio and demonstrate that it selectively modifies the model proteins streptavidin and avidin and the membrane protein BioY on cell surface. The reagent converts amines in the proximity of the binding pocket to azides and leaves the remaining amino groups in streptavidin untouched. Reagents of this novel class will find use in target identification as well as the selective functionalization and bioorthogonal protection of proteins.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.