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Updated: Nov 1, 2025

Engineering Antiviral Agents via Surface Plasmon Resonance

Engineering Antiviral Agents via Surface Plasmon Resonance

Published on: June 14, 2022

Engineered pH-Sensitive Protein G/IgG Interaction.

Ramesh K Jha¹, Allison Yankey¹, Kalifa Shabazz¹

¹Bioscience Division, Los Alamos National Laboratory, Los Alamos, New Mexico 87545, United States.

ACS Chemical Biology

|June 21, 2021

Summary

This summary is machine-generated.

Researchers engineered a pH-switchable protein interaction for Protein G/human IgG Fc domain (PrG/hIgG). This novel PrG-EHHE reagent offers controllable binding affinity, revolutionizing IgG purification by avoiding harsh acidic conditions.

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Last Updated: Nov 1, 2025

Engineering Antiviral Agents via Surface Plasmon Resonance

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Genetically-encoded Molecular Probes to Study G Protein-coupled Receptors

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Published on: September 13, 2013

Area of Science:

Protein Engineering
Biochemistry
Molecular Biology

Background:

Natural protein-protein interactions are complex and difficult to control.
Designing switchable protein interactions on demand remains a significant challenge in protein design.

Purpose of the Study:

To computationally redesign a natural protein interface for switchable pH-dependent binding.
To engineer a novel reagent for improved and controllable immunoglobulin G (IgG) purification.

Main Methods:

Computational redesign of the Protein G/human IgG Fc domain (PrG/hIgG) interface.
Introduction of histidine and glutamic acid residues onto Protein G (PrG-EHHE).
Assessing binding affinity changes with pH variation for PrG-EHHE and wild-type PrG (PrG-WT).

Main Results:

PrG-EHHE exhibited a 50-fold switch in binding affinity between mild acidic and mild basic pH.
The wild-type interface showed negligible pH-dependent binding changes.
PrG-EHHE demonstrated superior binding affinity under mild acidic conditions compared to PrG-WT.

Conclusions:

Engineered PrG-EHHE provides a novel pH-switchable protein interaction.
This engineered protein interaction can be revolutionary for IgG purification processes.
The ability to circumvent extreme acidic elution conditions offers a significant advantage in IgG purification.