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Monitoring Conformational Dynamics of Single Unmodified Proteins using Plasmonic Nanotweezers
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Responsive nanoprobes track membrane protein degradation during nanoparticle uptake. Dimeric proteins are endocytosed more efficiently, enhancing degradation and informing targeted nanoparticle drug delivery design.

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Area of Science:

  • Biomedical Engineering
  • Nanotechnology
  • Molecular Biology

Background:

  • Nanoparticle-mediated protein degradation is a promising biomedical tool.
  • Understanding dynamic processes is key to improving efficacy.
  • Distinguishing protein states (monomer vs. dimer) is crucial for targeted degradation.

Purpose of the Study:

  • Develop responsive plasmonic nanoprobes to observe membrane protein degradation.
  • Discriminate between monomeric and dimeric protein states during nanoparticle endocytosis.
  • Investigate the impact of protein aggregation state on degradation efficiency.

Main Methods:

  • Engineered aptamer-modified spherical nucleic acid nanoprobes for low-valence protein binding.
  • Utilized plasmonic coupling signals to detect protein dimerization and proximity.
  • Modeled degradation using the mesenchymal to epithelial transition factor (Met) protein.

Main Results:

  • Demonstrated differential endocytosis kinetics for monomeric and dimeric Met.
  • Observed enhanced endocytic efficiency for dimeric Met.
  • Showed aggregation-dependent enhancement of phosphorylated Met (p-Met) degradation.

Conclusions:

  • Responsive nanoprobes enable direct observation of membrane protein degradation.
  • Protein aggregation state influences nanoparticle-mediated degradation efficiency.
  • Findings provide a foundation for designing targeted protein degradation platforms.