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Related Experiment Video

Updated: Jun 11, 2026

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

Direct Dynamic Protein-Affinity Selection Mass-Spectrometry.

Niels Jonker¹, Henk Lingeman, Hubertus Irth

¹BioMolecular Analysis Group, Department of Chemistry, Faculty of Sciences, VU University Amsterdam, De Boelelaan 1083, 1081 HV Amsterdam, The Netherlands.

Chromatographia

|July 15, 2010

Summary

This study introduces a rapid affinity screening method for human estrogen receptor alpha ligand binding domain (ERalpha-LBD) interactions. The new technique significantly reduces analysis time, enabling faster identification of potential drug ligands.

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Published on: April 1, 2017

Area of Science:

Biochemistry
Analytical Chemistry
Pharmacology

Background:

Screening for ligands that interact with the human estrogen receptor alpha ligand binding domain (ERalpha-LBD) is crucial for drug discovery.
Existing methodologies often involve lengthy pre-concentration and chromatographic separation steps, limiting throughput and analysis time.

Purpose of the Study:

To develop and describe a novel, rapid affinity screening methodology for ERalpha-LBD ligands.
To significantly reduce the overall analysis time compared to existing methods.
To enable the determination of analytes with challenging chromatographic properties.

Main Methods:

In-solution incubation of analytes with His-tagged ERalpha-LBD.
Immobilization of the protein-ligand complex on a nickel-loaded protein-affinity selection column.
Elution of ligands using decreased pH and increased organic modifier, followed by MS detection; protein precipitation on a filter.

Main Results:

The developed methodology eliminates the need for pre-concentration and chromatographic separation.
Overall analysis time is reduced by approximately 250% to about 6 minutes.
The trapping column demonstrated reusability for at least 70 cycles.

Conclusions:

This new methodology offers a significantly faster and more efficient approach for ERalpha-LBD ligand affinity screening.
The method's ability to handle diverse analytes and its reduced analysis time make it advantageous for high-throughput screening.
The system's robustness, indicated by column reusability, supports its practical application in drug discovery.