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Updated: Jan 9, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
The Core-Shell Conformational Space of Compartmentalized Single-Chain Nanoparticles by Paramagnetic and
Federico Faglia1,2, Justus F Thümmler3, Christopher Pötzl1,2
1Faculty of Chemistry, Institute of Biological Chemistry, University of Vienna, Währinger Str. 38, Vienna, 1090, Austria.
Single-chain nanoparticles (SCNPs) form internal compartments like proteins. New NMR and simulation methods reveal their atomistic structure and functional mimicry.
Area of Science:
- Polymer Chemistry
- Nanotechnology
- Biomimetic Materials
Background:
- Single-chain nanoparticles (SCNPs) mimic protein size, structure, and function.
- Hierarchical folding in SCNPs can create internal compartments.
- Experimental determination of SCNP architecture is challenging.
Purpose of the Study:
- To dissect the conformational organization of amphiphilic SCNPs.
- To reveal internal compartmentalization and structure at atomistic resolution.
- To introduce a transferable methodology for probing synthetic macromolecule compartmentalization.
Main Methods:
- Paramagnetic NMR spectroscopy.
- Hyperpolarized water-based dissolution dynamic nuclear polarization (d-DNP).
- NMR-guided molecular dynamics simulations.
Main Results:
- Detailed intramolecular structures and solvent accessibility were mapped.
- Distinct nanoscopic compartments formed by PEG side chain back-folding were identified.
- Internal segments were shielded, mimicking enzyme hydrophobic pockets.
Conclusions:
- A transferable methodology for probing functional compartmentalization in synthetic macromolecules was established.
- This work provides a tool for designing enzyme mimetics and nanomaterials with programmable order.
- High-resolution structural information of hierarchically structured SCNPs was obtained.
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