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Journal article
Engineered pH-Sensitive Protein G/IgG Interaction
ACS chemical biology, v 16(7), pp 1142-1146
16 Jul 2021
PMID: 34152722
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
While natural protein-protein interactions have evolved to be induced by complex stimuli, rational design of interactions that can be switched-on-demand still remain challenging in the protein design world. Here, we demonstrate that a computationally redesigned natural interface for improved binding affinity could further be mutated to adopt a pH switchable interaction. The redesigned interface of Protein G/human IgG Fc domain (referred to as PrG/hIgG), when incorporated with histidine and glutamic acid on PrG (PrG-EHHE), showed a switch in binding affinity by 50-fold when the pH was altered from mild acidic to mild basic. The wild-type (WT) interface showed a negligible switch. The overall binding affinity under mild acidic pH for PrG-EHHE outperformed the wild-type PrG (PrG-WT) interaction. The new reagent PrG-EHHE can be revolutionary in IgG purification, since the standard method of using an extreme acidic pH for elution can be circumvented.
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Details
- Title
- Engineered pH-Sensitive Protein G/IgG Interaction
- Creators
- Ramesh K. Jha - Los Alamos National LaboratoryAllison Yankey - Drexel UniversityKalifa Shabazz - Los Alamos National LaboratoryLeslie Naranjo - Los Alamos National LaboratorySang-Min Shin - Los Alamos Natl Lab, Biosci Div, Los Alamos, NM 87545 USANileena Velappan - Los Alamos National LaboratoryAndrew R. M. Bradbury - Los Alamos Natl Lab, Biosci Div, Los Alamos, NM 87545 USACharlie E. M. Strauss - Los Alamos National Laboratory
- Publication Details
- ACS chemical biology, v 16(7), pp 1142-1146
- Publisher
- Amer Chemical Soc
- Number of pages
- 5
- Grant note
- 89233218CNA000001 / U.S. Department of Energy National Nuclear Security Administration; National Nuclear Security Administration; United States Department of Energy (DOE) 89233218CNA000001 / U.S. Department of Energy; United States Department of Energy (DOE)
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- College of Medicine
- Web of Science ID
- WOS:000674917600004
- Scopus ID
- 2-s2.0-85110386712
- Other Identifier
- 991021860762904721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology