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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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Insights into the Interactions of Amino Acids and Peptides with Inorganic Materials Using Single-Molecule Force Spectroscopy

Insights into the Interactions of Amino Acids and Peptides with Inorganic Materials Using Single-Molecule Force Spectroscopy

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Estimation of Molecular Interaction Force Using Atomic Force Microscopy for Bioapplication.

Hweiyan Tsai^1,2, Zihkai Chen³, Huiwen Deng³

¹School of Medical Applied Chemistry, Chung Shan Medical University , Taichung 402 Taiwan.

The Journal of Physical Chemistry. B

|October 19, 2016

Summary

This summary is machine-generated.

This study presents an optimized atomic force microscopy method to measure molecular interaction forces for bioapplications. The technique accurately quanties forces for protein-ligand and antibody-antigen interactions, crucial for biosensing and surface studies.

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Investigating Single Molecule Adhesion by Atomic Force Spectroscopy

Investigating Single Molecule Adhesion by Atomic Force Spectroscopy

Published on: February 27, 2015

Area of Science:

Biophysics
Surface Science
Nanotechnology

Background:

Estimating molecular interaction forces is vital for understanding biological processes.
Current methods for measuring these forces can be challenging, especially for bioapplications.
Atomic Force Microscopy (AFM) offers a potential avenue for precise force measurements.

Purpose of the Study:

To develop and optimize an AFM-based method for estimating molecular interaction forces.
To validate the method using well-characterized molecular pairs.
To explore the potential of this technique for various bioanalytical applications.

Main Methods:

Utilized Atomic Force Microscopy (AFM) to measure molecular interaction forces.
Optimized experimental parameters including tip/substrate labeling concentrations and loading rates.
Applied the method to three model molecular systems: IgG/anti-IgG, BSA/anti-BSA, and streptavidin/biotin.

Main Results:

Successfully estimated molecular interaction forces for IgG/anti-IgG (121 ± 3 pN), BSA/anti-BSA (185 ± 4 pN), and streptavidin/biotin (241 ± 4 pN).
Obtained consistent measurements within the range reported in existing literature.
Demonstrated the feasibility of force estimation from force-distance curves in bioapplications.

Conclusions:

The optimized AFM method provides a reliable approach for quantifying molecular interaction forces.
This technique holds significant potential for diverse bioapplications, including protein-ligand and antibody-antigen studies.
The method can also aid in investigating the properties of molecular, cellular, and bacterial surfaces.