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Synthesis and Bioconjugation of Thiol-Reactive Reagents for the Creation of Site-Selectively Modified Immunoconjugates
Published on: March 6, 2019
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Tyrosine bioconjugation - an emergent alternative
Peter A Szijj1, Kristina A Kostadinova1, Richard J Spears1
1Department of Chemistry, University College London, London, UK. v.chudasama@ucl.ac.uk.
Organic & Biomolecular Chemistry
|November 3, 2020
Summary
Tyrosine bioconjugation offers a powerful alternative to traditional protein modification methods like cysteine and lysine bioconjugation. This approach enables precise, dual modifications for advanced applications in therapeutics and biomaterials.
Area of Science:
- Biochemistry
- Chemical Biology
- Materials Science
Background:
- Protein bioconjugation is crucial for therapeutics and biomaterials.
- Cysteine and lysine bioconjugation are established but have limitations.
- Dual modification of proteins is increasingly desired but challenging.
Purpose of the Study:
- To review tyrosine bioconjugation as an emerging strategy.
- To highlight recent advancements in tyrosine bioconjugation methods.
- To assess its compatibility with existing bioconjugation techniques.
Main Methods:
- Review of existing literature on protein bioconjugation.
- Focus on recent developments in tyrosine-specific modification.
- Analysis of chemoselectivity and conversion rates.
Main Results:
- Tyrosine bioconjugation is a viable alternative and complement to cysteine and lysine methods.
- Recent methods demonstrate high conversion and chemoselectivity.
- Tyrosine modification can be combined with other strategies for dual conjugation.
Conclusions:
- Tyrosine bioconjugation is a rapidly advancing field.
- It facilitates the creation of complex, multi-modified proteins.
- This technique expands possibilities in protein engineering and applications.
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