Single-Molecule Rotation for EGFR Conformational Dynamics in Live Cells

J Am Chem Soc. 2018 Nov 14;140(45):15161-15165. doi: 10.1021/jacs.8b09037. Epub 2018 Nov 2.

Abstract

Monitoring the dynamics of proteins in live cells on appropriate spatiotemporal scales may provide key information regarding long-standing questions in molecular and cellular regulatory mechanisms. However, tools capable of imaging the conformational changes over time have been elusive. Here, we present a single-molecule stroboscopic imaging probes by developing gyroscopic plasmonic nanoparticles, allowing for replication of protein-protein interactions and the conformational dynamics based on rotational and lateral velocities. This study fundamentally monitors the rotational motion of a membrane protein, epidermal growth factor receptor (EGFR), to decipher undiscovered structural dynamics in live cells without any molecular perturbations. This method offers a strategy to visualize assemblies and conformational changes, and provides unique insights into the mechanism underlying the molecular dynamics for receptors.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Line
  • ErbB Receptors / chemistry
  • Humans
  • Molecular Dynamics Simulation*
  • Protein Binding
  • Protein Conformation

Substances

  • EGFR protein, human
  • ErbB Receptors