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Related Concept Videos

Atomic Force Microscopy01:08

Atomic Force Microscopy

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The cytoskeletal architecture can be studied using different microscopic and biochemical techniques. Electron microscopy was instrumental in discovering the cytoskeletal architecture around the 1960s, which allowed obtaining structural information at a high-resolution level. However, the sample preparation procedure often limits this ability in biological samples. Several protocols have been developed over the years to optimize sample preparation. In one of the protocols known as rotary...
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Related Experiment Video

Updated: Nov 13, 2025

Force Spectroscopy of Single Protein Molecules Using an Atomic Force Microscope
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High-speed atomic force microscopy to study pore-forming proteins.

Fang Jiao1, Yi Ruan2, Simon Scheuring1

  • 1Department of Anesthesiology, Weill Cornell Medicine, New York, NY, United States; Department of Physiology and Biophysics, Weill Cornell Medicine, New York, NY, United States.

Methods in Enzymology
|March 13, 2021
PubMed
Summary
This summary is machine-generated.

Pore-forming proteins (PFPs) damage cell membranes. High-speed atomic force microscopy (HS-AFM) visualized real-time dynamics of PFP pore formation, revealing distinct mechanisms for Listeriolysin O, lysenin, and Perforin-2.

Keywords:
Conformational changesDynamicsHS-AFMHigh-speed atomic force microscopyLLOListeriolysin OLyseninPFN2PFPPerforin-2PorePore-forming proteinPre-poreSLBSupported lipid bilayerToxin

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Area of Science:

  • Biophysics
  • Molecular Biology
  • Cell Biology

Background:

  • Pore-forming proteins (PFPs) are crucial in various biological processes, from pathogenicity to apoptosis.
  • While structures of PFPs are known, the dynamics of their membrane insertion and pore formation remain poorly understood.
  • Existing techniques lack the resolution to visualize these dynamic transitions in real-time.

Purpose of the Study:

  • To investigate the real-time dynamics of pore formation in various PFPs using high-speed atomic force microscopy (HS-AFM).
  • To elucidate the conformational transitions from pre-pore to pore states and the kinetics of oligomerization.
  • To provide detailed protocols for HS-AFM studies of PFPs on lipid bilayers.

Main Methods:

  • Utilized high-speed atomic force microscopy (HS-AFM) for real-time, real-space imaging of PFP-membrane interactions.
  • Prepared supported lipid bilayers for controlled experimental conditions.
  • Studied Listeriolysin O (LLO), lysenin, and Perforin-2 (PFN2) under varying conditions.

Main Results:

  • HS-AFM visualized distinct pore formation mechanisms for different PFPs.
  • LLO formed membrane-damaging arcs, while lysenin formed stable nonameric rings.
  • PFN2 exhibited rapid pH-dependent pre-pore to pore transitions within 3 seconds.

Conclusions:

  • HS-AFM is a powerful tool for real-time observation of PFP dynamics.
  • PFPs exhibit diverse mechanisms of membrane permeabilization.
  • Understanding these dynamics is crucial for deciphering PFP function and developing targeted interventions.