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Nano-Differential Scanning Fluorimetry for Screening in Fragment-based Lead Discovery

Nano-Differential Scanning Fluorimetry for Screening in Fragment-based Lead Discovery

Published on: May 16, 2021

A quantitative affinity-based technique for the identification of potential lead compounds.

Tomonori Arai¹, Masayoshi Uehata, Hiroyuki Akatsuka

¹Discovery Screening Center, Mitsubishi Tanabe Pharma, Saitama 335-8505, Japan. arai.tomonori@me.mt-pharma.co.jp

Analytical Biochemistry

|January 30, 2013

Summary

A new quantitative size-exclusion chromatography/liquid chromatography/mass spectrometry (qSEC-LC/MS) method rapidly evaluates protein-compound interactions. This affinity-based technique shows promise for drug discovery, though K(d) determination requires further refinement.

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Area of Science:

Biochemistry
Analytical Chemistry
Pharmacology

Background:

Accurate quantification of protein-compound interactions is crucial for drug discovery.
Existing methods can be time-consuming or require large sample volumes.
There is a need for rapid, high-throughput analytical techniques.

Purpose of the Study:

To develop and validate a quantitative analytical method for rapid evaluation of protein-compound interactions.
To establish a high-throughput assay for binding affinity determination.
To demonstrate the utility of the method using a model system.

Main Methods:

Development of a quantitative size-exclusion chromatography (qSEC) method.
Integration with liquid chromatography/mass spectrometry (LC/MS) for compound quantification.
Assay performed in a 96-well format for high-throughput screening.
Validation using a thrombin-inhibitor model system.

Main Results:

The qSEC-LC/MS method was successfully developed and validated.
The assay quantifies bound compound as an indicator of binding affinity.
Proof of concept demonstrated effective affinity-based analysis.
The method showed potential as a rapid screening tool.

Conclusions:

The qSEC-LC/MS method provides a rapid and effective approach for evaluating protein-compound interactions.
This technique can be valuable for drug discovery and development.
Further optimization may be needed for precise K(d) value determination.