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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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Related Experiment Video

Updated: Jul 9, 2026

Investigating Receptor-ligand Systems of the Cellulosome with AFM-based Single-molecule Force Spectroscopy

Investigating Receptor-ligand Systems of the Cellulosome with AFM-based Single-molecule Force Spectroscopy

Published on: December 20, 2013

Reverse engineering of an affinity-switchable molecular interaction characterized by atomic force microscopy

Dario Anselmetti¹, Frank Wilco Bartels, Anke Becker

¹Experimental Biophysics & Applied Nanoscience, Department of Physics, Bielefeld University, Bielefeld, Germany. dario.anselmetti@physik.uni-bielefeld.de

Langmuir : the ACS Journal of Surfaces and Colloids

|December 8, 2007

Summary

Researchers developed a switchable molecular system mimicking cellular control. This system, tunable with light and heat, demonstrates controllable molecular interactions for future applications in molecular memories and artificial ion channels.

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Last Updated: Jul 9, 2026

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Published on: December 20, 2013

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Published on: February 27, 2015

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

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Area of Science:

Molecular biology
Biophysics
Synthetic chemistry

Background:

Tunable molecular interactions are crucial for cellular process regulation.
Reverse molecular engineering aims to create synthetic molecules mimicking biological functions.

Purpose of the Study:

To quantitatively investigate autoinducer-regulated DNA-protein interactions in bacterial gene regulation.
To develop an artificial bistable molecular system controllable by external signals.

Main Methods:

Single-molecule force spectroscopy using atomic force microscopy (AFM).
Development of an artificial host-guest system responsive to UV light and thermal energy.

Main Results:

Demonstrated quantitative investigation of DNA-protein interactions at the single-molecule level.
Successfully developed a bistable molecular system with externally controlled switching.
Verified reproducible and reversible switching of intermolecular binding affinity using AFM.

Conclusions:

The developed affinity-tunable optomechanical switch enables precise control over molecular interactions.
Potential applications include molecular manipulation, rewritable molecular memories, and artificial ion channels for controlled transport.