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Antibody Structure

Antibody Structure

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Assessment of Stress Effects on Cognitive Flexibility using an Operant Strategy Shifting Paradigm

Assessment of Stress Effects on Cognitive Flexibility using an Operant Strategy Shifting Paradigm

Published on: May 4, 2020

pH-shift stress on antibodies.

Hiroshi Imamura¹, Shinya Honda²

¹Biomedical Research Institute, National Institute of Advanced Industrial Science and Technology, Tsukuba, Japan; Department of Applied Chemistry, College of Life Sciences, Ritsumeikan University, Kusatsu, Japan.

Methods in Enzymology

|June 4, 2019

Summary

This summary is machine-generated.

This study introduces a pH-shift technique to assess antibody aggregation. This method separates unfolding and aggregation, enabling better evaluation of antibody stability for pharmaceutical quality control.

Keywords:

Aggregation Antibody Light scattering Unfolding pH-shift stress

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Area of Science:

Biochemistry
Pharmaceutical Science
Protein Chemistry

Background:

Antibody unfolding and aggregation are critical concerns in pharmaceutical development, impacting drug quality and efficacy.
Current stress assays often induce unfolding and aggregation concurrently, complicating the analysis of aggregation mechanisms.
High-quality pharmaceutical antibodies necessitate robust methods for evaluating their stability and aggregation propensity.

Purpose of the Study:

To introduce a novel pH-shift stress assay for evaluating antibody aggregation.
To enable the assessment of antibody aggregation under conditions that separate unfolding and aggregation steps.
To provide a method for assessing antibody aggregation at neutral pH and ambient temperature.

Main Methods:

Antibodies were subjected to a pH-shift stress, involving initial unfolding in a low pH solution.
A subsequent neutralization step was employed to induce refolding and aggregation.
Light scattering analysis was utilized to monitor and quantify antibody aggregation.

Main Results:

The pH-shift technique successfully induced antibody unfolding and subsequent aggregation.
This method allowed for the separation of unfolding and aggregation processes.
The assay demonstrated the ability to evaluate antibody aggregation at neutral pH and ambient temperature.

Conclusions:

The described pH-shift technique is a valuable tool for assessing antibody aggregation.
This method offers an advantage by preventing the simultaneous generation of unfolded molecules during aggregation.
The assay facilitates the evaluation of antibody stability and aggregation propensity for pharmaceutical applications.