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Assays for the Degradation of Misfolded Proteins in Cells

Assays for the Degradation of Misfolded Proteins in Cells

Published on: August 28, 2016

High throughput methods of assessing protein stability and aggregation.

Guillermo A Senisterra¹, Patrick J Finerty

¹Structural Genomics Consortium, Suite 700, 7th Floor, MaRS South Tower, 101 College St., Toronto, ON M51L7, Canada. g.senisterra@utoronto.ca

Molecular Biosystems

|February 20, 2009

Summary

Developing multi-sample methods is crucial for identifying protein stability and aggregation conditions. These techniques aid in protein purification, crystallization, and drug discovery by screening compounds that interact with proteins.

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Area of Science:

Biochemistry and structural biology
Protein science and drug discovery

Background:

Increasing demand for purified proteins necessitates efficient methods for structural studies.
Protein stability and aggregation are critical factors influencing purification and crystallization success.

Purpose of the Study:

To present and discuss multi-sample methods for assessing protein stability and aggregation.
To highlight the utility of these methods in identifying stabilizing conditions and potential drug candidates.

Main Methods:

Differential Scanning Fluorimetry (DSF)
Differential Static Light Scattering (DSLS)
Isothermal Denaturation (ITD)

Main Results:

The article describes three distinct techniques for measuring protein stability and aggregation.

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These methods enable the screening of solution conditions and small molecules.

Identified stabilizing conditions can enhance protein purification and crystallization outcomes.

Conclusions:

Multi-sample methods are essential for optimizing protein studies and advancing drug discovery.
Differential Scanning Fluorimetry, Differential Static Light Scattering, and Isothermal Denaturation offer valuable approaches.
These techniques facilitate the identification of protein-ligand interactions and stabilizing agents.