Multimerization interactions between protein-inspired single-chain random heteropolymers
Shayna L Hilburg1, Tianyi Jin1,2, Priya Ganesh1
1Department of Materials Science and Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts, United States of America.
Plos One
|May 28, 2026
Summary
Single-chain nanoparticles (SCNPs) mimic proteins by forming multimers through side-chain interactions. Their conformation significantly influences multimerization, not sequence variation.
Area of Science:
- Polymer Chemistry
- Biomaterials Science
- Computational Chemistry
Background:
- Single-chain nanoparticles (SCNPs) exhibit protein-like behaviors, making them promising for various applications.
- Understanding SC NP interactions with other macromolecules is crucial for designing advanced materials.
Purpose of the Study:
- To investigate the interaction mechanisms of SC Nps with other macromolecules using molecular dynamics simulations.
- To characterize the multimerization behavior of methacrylate-based SC Nps in aqueous solutions.
Main Methods:
- Molecular dynamics simulations were employed to model SC NP behavior.
- Analysis focused on non-covalent assembly driven by hydrophobic effects and Flory-Huggins parameters.
- Interaction modes and monomer enrichment at contact points were examined.
Main Results:
- SC Nps demonstrated two main interaction modes: adsorption via side-chain interactions (similar to protein oligomerization) and maintenance of single-chain structures.
- Amphiphilic monomers, particularly hydrophobic residues, enriched at contact interfaces during prolonged adsorption.
- Polymer conformation played a significant role in multimerization, outweighing sequence variations.
Conclusions:
- SC Nps can undergo multimerization through protein-like adsorption mechanisms.
- The conformational dynamics of SC Nps are key determinants of their self-assembly and interaction behavior.
- These findings provide insights into designing SC Nps for targeted macromolecular interactions.
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