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Atomic Force Microscopy

Atomic Force Microscopy

Atomic force microscopy (AFM) is a type of scanning probe microscopy that can analyze topographic details of various specimens like ceramics, glass, polymers, and biological samples. AFM offers over 1000 times more resolution than the optical imaging system. Images generated from AFM are three-dimensional surface profiles, offering an advantage over the flat, two-dimensional images from other imaging techniques.
The AFM Probe
The probe is regarded as the heart of any AFM setup and comprises the...

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Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

Published on: September 12, 2019

Testing synthetic amyloid-β aggregation inhibitor using single molecule atomic force spectroscopy.

Francis T Hane¹, Brenda Y Lee¹, Anahit Petoyan²

¹University of Waterloo, Department of Biology, 200 University Ave. West, Waterloo, Ontario, Canada N2L 3G1.

Biosensors & Bioelectronics

|December 11, 2013

Summary

Researchers tested SG1, a novel inhibitor, to prevent amyloid-β aggregation in Alzheimer's disease. Single-molecule atomic force spectroscopy confirmed SG1

Keywords:

Aggregation inhibitor Alzheimer's disease Amyloid-β aggregation Fibril formation Molecular dynamics simulations Single molecule force spectroscopy

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OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy

Published on: February 5, 2020

Area of Science:

Neuroscience
Biochemistry
Biophysics

Background:

Alzheimer's disease is a neurodegenerative disorder with limited treatment options.
Amyloid-β peptide oligomers are the primary neurotoxic agents.
Inhibiting amyloid aggregation is a key therapeutic strategy.

Purpose of the Study:

To evaluate a novel pseudopeptidic aggregation inhibitor, SG1.
To investigate SG1's ability to prevent amyloid-β misfolding.
To establish single-molecule atomic force spectroscopy as a method for assessing inhibitor efficacy.

Main Methods:

Utilized single-molecule atomic force spectroscopy (smAFM).
Quantified binding forces between individual amyloid-β peptide molecules.
Measured the experimental yield of binding to assess inhibitor effectiveness.

Main Results:

Demonstrated that SG1 binds to the amyloid-β self-recognition site.
Showed SG1 prevents amyloid-β from forming β-sheet structures.
Confirmed smAFM can measure the efficacy of amyloid aggregation inhibitors.

Conclusions:

SG1 is a promising inhibitor of amyloid-β aggregation.
Single-molecule atomic force spectroscopy is a viable technique for screening anti-amyloid drugs.
This method offers a new approach for rapid assessment of inhibitor drug efficacy.