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Effects of Arginine on Hierarchical Protein Aggregation
Suguru Nishinami1,2, Yoshiki Kihara3, Teruo Akuta4
1Institute of Pure and Applied Sciences, University of Tsukuba, Tsukuba, Japan. nishinami@igm.hokudai.ac.jp.
The Protein Journal
|February 20, 2026
Summary
Arginine prevents insoluble protein aggregates but promotes soluble ones by modulating interactions. This suggests a new model for protein aggregation, crucial for understanding diseases like Alzheimer's.
Area of Science:
- Biochemistry
- Protein Chemistry
- Pharmaceutical Sciences
Background:
- Arginine is a common excipient in protein formulations to prevent aggregation.
- The precise mechanisms by which arginine influences protein aggregation pathways are not fully understood.
Purpose of the Study:
- To investigate the effects of arginine on heat- and acid-induced protein aggregation.
- To elucidate the role of arginine in modulating soluble versus insoluble aggregate formation.
Main Methods:
- Studied heat- and acid-induced aggregation of immunoglobulin G (IgG).
- Examined heat-induced aggregation of various model proteins.
- Analyzed the impact of arginine on aggregate formation and monomer recovery.
Main Results:
- Arginine suppressed insoluble aggregate formation but had minimal effect on monomer recovery.
- Arginine promoted the formation of soluble protein aggregates.
- A hierarchical aggregation model was proposed, where arginine modulates intermolecular interactions.
Conclusions:
- Arginine differentially affects protein aggregation pathways, favoring soluble aggregate formation.
- Soluble aggregate formation is a common phenomenon across diverse proteins.
- Understanding soluble aggregates may provide insights into disease-related protein assemblies.
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