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Updated: Jun 15, 2025

NMR-Based Fragment Screening in a Minimum Sample but Maximum Automation Mode

NMR-Based Fragment Screening in a Minimum Sample but Maximum Automation Mode

Published on: June 4, 2021

Protocol to perform fragment screening using NMR spectroscopy.

Qiwei Huang¹, CongBao Kang¹

¹Experimental Drug Development Centre (EDDC), Agency for Science, Technology and Research (A∗STAR), Singapore 138670, Singapore.

|August 23, 2024

Summary

This summary is machine-generated.

This study details a nuclear magnetic resonance (NMR) spectroscopy protocol for fragment screening. It enables efficient identification and mapping of small molecule binders to proteins like Kirsten rat sarcoma viral oncogene homolog (KRAS).

Keywords:

NMR high-throughput screening protein expression and purification

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Area of Science:

Biochemistry
Structural Biology
Drug Discovery

Background:

Fragment-based drug design is crucial for identifying novel therapeutics.
Protein-observed NMR spectroscopy is a powerful technique for studying protein-ligand interactions.
Isotopically labeled proteins are essential for NMR-based screening.

Purpose of the Study:

To present a comprehensive protocol for fragment screening using NMR spectroscopy.
To demonstrate the application of this protocol for Kirsten rat sarcoma viral oncogene homolog (KRAS) G12D protein.
To enable mapping of ligand-binding sites and determination of binding affinities.

Main Methods:

Production of 15N-labeled KRAS G12D protein.
Fragment screening utilizing 1H-15N-heteronuclear single quantum coherence (HSQC) experiments.
Fragment deconvolution, binding affinity determination, and binding site mapping.

Main Results:

A robust protocol for fragment screening via NMR was established.
The protocol successfully identified potential binders to KRAS G12D.
Detailed mapping of fragment-binding sites was achieved.

Conclusions:

This NMR-based fragment screening protocol offers a valuable strategy for drug discovery.
The method facilitates the characterization of protein-ligand interactions.
It aids in the development of targeted therapeutics by mapping binding sites.