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Updated: Dec 7, 2025

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

Sequential dual site-selective protein labelling enabled by lysine modification.

Maria J Matos¹, Libby Brown¹, Barbara Bernardim¹

¹Department of Chemistry, University of Cambridge, Lensfield Road, CB2 1EW Cambridge, UK.

Bioorganic & Medicinal Chemistry

|October 2, 2020

Summary

This summary is machine-generated.

This study introduces a novel method for dual protein modification, achieving site-selective labeling at lysine, cysteine, and ketone sites. This breakthrough enables the creation of functional, precisely engineered proteins for various applications.

Keywords:

Albumin Antibodies Bioorthogonal labelling Lysine modification Protein modification

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Last Updated: Dec 7, 2025

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry

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Published on: April 4, 2018

Specificity Analysis of Protein Lysine Methyltransferases Using SPOT Peptide Arrays

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Published on: November 29, 2014

Area of Science:

Chemical Biology
Protein Engineering
Bioconjugation Chemistry

Background:

Chemical site-selective dual protein modification methods are limited.
Orthogonal strategies are crucial for precise protein labeling.

Purpose of the Study:

To demonstrate the orthogonality and compatibility of regioselective lysine modification with cysteine and ketone-based labeling.
To develop a sequential, orthogonal approach for dual site-selective protein modification.

Main Methods:

Regioselective lysine modification.
Protein modification at cysteine residues.
Utilizing genetically encoded ketone-tagged amino acids.
Sequential and orthogonal labeling strategies.

Main Results:

Proof-of-concept for orthogonal and compatible dual modification.
Successful application to albumin and a therapeutic antibody.
Creation of functional, dual site-selectively labeled proteins.

Conclusions:

The developed sequential, orthogonal method enables precise dual site-selective protein modification.
This approach expands the toolkit for engineering functional proteins with tailored properties.