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Related Experiment Video

Updated: Sep 21, 2025

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

Published on: September 12, 2019

Measuring Protein Aggregation and Stability Using High-Throughput Biophysical Approaches.

Tristan O C Kwan¹, Stefan A Kolek², Amy E Danson¹

¹National Physical Laboratory, Teddington, United Kingdom.

Frontiers in Molecular Biosciences

|June 2, 2022

Summary

This summary is machine-generated.

Improving recombinant protein stability and reducing aggregation is key for research and drug discovery. High-throughput biophysical methods accelerate the identification of optimal conditions, enhancing sample quality and reducing costs.

Keywords:

CD DLS DSF cryo-EM crystallography drug discovery high-throughput protein aggregation

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Last Updated: Sep 21, 2025

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

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Published on: September 12, 2019

Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans

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Published on: December 17, 2021

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Published on: April 5, 2013

Area of Science:

Biochemistry
Biophysics
Drug Discovery

Background:

Protein structure-function relationships are vital for biochemistry, medical research, and drug discovery.
Recombinant protein production for research and biopharmaceuticals is often limited by instability and aggregation in vitro.
Poor protein sample quality leads to reduced reproducibility and increased research expenses.

Purpose of the Study:

To discuss workflows for improving protein stability and reducing aggregation.
To adapt established biophysical methods for high-throughput screening.
To accelerate the identification and optimization of conditions that enhance protein integrity.

Main Methods:

Adapting established biophysical methods for high-throughput screening (HTS).
Implementing workflows for rapid identification of stabilizing conditions.
Utilizing HTS to assess protein aggregation and stability.

Main Results:

Workflows enabling rapid identification of conditions promoting protein stability.
Optimization strategies to minimize protein aggregation.
Enhanced protein sample quality, stability, and reproducibility.

Conclusions:

High-throughput biophysical screening accelerates the discovery of optimal conditions for protein stability.
Improved protein quality reduces research and development time and costs.
These approaches support both fundamental research and industrial biopharmaceutical development.