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Related Concept Videos

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Protein-protein Interfaces

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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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Protein Networks02:26

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An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
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Single-Molecule Observation of Competitive Protein-Protein Interactions Utilizing a Nanopore.

Jiaxin Sun1, Antun Skanata1,2, Liviu Movileanu1,2,3,4

  • 1Department of Physics, Syracuse University, 201 Physics Building, Syracuse, New York 13244-1130, United States.

ACS Nano
|December 24, 2024
PubMed
Summary

This study introduces a novel nanopore sensor to track competitive protein-ligand interactions in real-time. It allows researchers to observe how different proteins bind to a receptor one by one, overcoming limitations of previous methods.

Keywords:
ion channelprotein dynamicsprotein engineeringprotein hubsingle-molecule electrophysiology

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Area of Science:

  • Biophysics
  • Molecular Biology
  • Cell Signaling

Background:

  • Protein-protein interactions (PPIs) are crucial for cell signaling.
  • Existing technologies struggle to analyze competitive binding kinetics due to ensemble averaging and limited time resolution.
  • Disentangling simultaneous interactions of multiple ligands with a single receptor is a significant challenge.

Purpose of the Study:

  • To develop a label-free method for dissecting the kinetic complexity of competitive protein-ligand interactions.
  • To enable single-molecule analysis of transient binding events.
  • To provide a platform for understanding complex PPIs and aiding drug development.

Main Methods:

  • Utilized a genetically encoded nanopore sensor for label-free, single-molecule detection.
  • Employed the resistive-pulse technique to monitor kinetics and dynamics of reversible PPIs.
  • Used binary mixtures of protein ligands with varying affinities against a common receptor immobilized on a nanopore tip.

Main Results:

  • Successfully disentangled competitive PPIs in a one-on-one manner.
  • Monitored the sequential binding and unbinding of individual protein ligands to a receptor.
  • Quantitatively compared single-molecule data with a two-ligand, one-receptor queuing model.

Conclusions:

  • The developed nanopore sensor provides a high-time bandwidth method to study competitive PPIs.
  • This approach overcomes ensemble averaging limitations, offering mechanistic insights into complex binding events.
  • The technology can advance drug discovery for targets involving protein hubs and complex PPI networks.