Evolution of Chemistry for Precision Engineering of Proteins

Ragendu, V.; Kumar, Mohan; Molla, Rajib; Thakur, K. B.; Chauhan, Preeti; Rai, Vishal

doi:10.51167/acm00047

AsiaChem Magazine 2023

DOI: 10.51167/acm00047

|View full text |Cite

Evolution of Chemistry for Precision Engineering of Proteins

V. Ragendu

Mohan Kumar

Rajib Molla

et al.

Abstract: Biophysical investigations require the covalent tagging of proteins to study their structure, dynamics, and biomolecular interactions. 1 A promising approach for the same involves tethering protein with the probe of interest. 2,3,4 For example, the installation of fluorophore and fluorescence

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...

Citation Types

Supporting

Mentioning

Contrasting

Year Published

2024

Publication Types

Select...

Article1

Relationship

Self Cite0

Independent1

Authors

Journals

Cited by 1 publication

References 118 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

Thermally Triggered Triazolinedione–Tyrosine Bioconjugation with Improved Chemo- and Site-Selectivity

Denijs,

Unal,

Bevernaege

et al. 2024

J. Am. Chem. Soc.

View full text Add to dashboard Cite

A bioconjugation strategy is reported that allows the derivatization of tyrosine side chains through triazolinedione-based "Y-clicking". Blocked triazolinedione reagents were developed that, in contrast to classical triazolinedione reagents, can be purified before use, can be stored for a long time, and allow functionalization with a wider range of cargoes and labels. These reagents are benchstable at room temperature but steadily release highly reactive triazolinediones upon heating to 40 °C in buffered media at physiological pH, showing a sharp temperature response over the 0 to 40 °C range. This conceptually interesting strategy, which is complementary to existing photo-or electrochemical bioorthogonal bond-forming methods, not only avoids the classical synthesis and handling difficulties of these highly reactive click-like reagents but also markedly improves the selectivity profile of the tyrosine conjugation reaction itself. It avoids oxidative damage and "off-target" tryptophan labeling, and it even improves site-selectivity in discriminating between different tyrosine side chains on the same protein or different polypeptide chains. In this research article, we describe the stepwise development of these reagents, from their short and modular synthesis to small-molecule model bioconjugation studies and proof-of-principle bioorthogonal chemistry on peptides and proteins.

show abstract

Thermally Triggered Triazolinedione–Tyrosine Bioconjugation with Improved Chemo- and Site-Selectivity

Denijs,

Unal,

Bevernaege

et al. 2024

J. Am. Chem. Soc.

View full text Add to dashboard Cite

show abstract

scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.

Contact Info

customersupport@researchsolutions.com

10624 S. Eastern Ave., Ste. A-614

Henderson, NV 89052, USA

This site is protected by reCAPTCHA and the Google Privacy Policy and Terms of Service apply.

Blog Terms and Conditions API Terms Privacy Policy Contact Cookie Preferences Do Not Sell or Share My Personal Information

Made with 💙 for researchers

Part of the Research Solutions Family.

Evolution of Chemistry for Precision Engineering of Proteins

Cited by 1 publication

References 118 publications

Thermally Triggered Triazolinedione–Tyrosine Bioconjugation with Improved Chemo- and Site-Selectivity

Thermally Triggered Triazolinedione–Tyrosine Bioconjugation with Improved Chemo- and Site-Selectivity

Contact Info

Product

Resources

About