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Updated: May 23, 2025

Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro
Published on: April 8, 2020
Design of Multimodal Supramolecular Protein Assemblies via Enzyme-Substrate Interactions for Intracellular
Xiaoxuan Yu1,2, Hui Li1,2, Jiarun Wu1
1Key Laboratory of Organosilicon Chemistry and Material Technology, Ministry of Education, Zhejiang Key Laboratory of Organosilicon Material Technology, College of Material, Chemistry and Chemical Engineering, Hangzhou Normal University, Hangzhou 311121, Zhejiang, China.
None:
Allosteric modulation of protein function, which involves effector binding triggering distant conformational changes, is crucial for cellular and metabolic control. However, achieving tunable control, structural diversity, and precise intracellular regulation remains challenging. Here, we designed dynamic supramolecular protein assemblies driven by enzyme-substrate interactions for antioxidant regulation in cells. Using a glutathione S-transferase modified with a cysteine mutation (GSTK77C), we engineered an effector molecule (GMP4M) containing a glutathione (GSH) moiety and maleimide group linked by a PEG chain. This system forms hierarchical protein assemblies with diverse morphologies, including nanowires, nanorings, nanobranches, and nanotwists, and switchable "ON/OFF" enzymatic activity modulated by endogenous GSH. The assemblies maintain structural integrity under physiological conditions, show remarkable reversibility, and outperform native GST in stability and environmental adaptability. This approach provides a versatile platform for creating tunable and diverse protein assemblies with broad applications in antioxidant therapies and biomedical interventions.
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