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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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Visualization of Recombinant DNA and Protein Complexes Using Atomic Force Microscopy

Visualization of Recombinant DNA and Protein Complexes Using Atomic Force Microscopy

Published on: July 18, 2011

Monoclonal antibody aggregation intermediates visualized by atomic force microscopy.

Hanjoo Lee¹, Marc Kirchmeier, Henryk Mach

¹Merck Research Laboratories, West Point, Pennsylvania 19486, USA.

Journal of Pharmaceutical Sciences

|July 24, 2010

Summary

Therapeutic protein aggregation, a common issue in antibody treatments, is better understood using atomic force microscopy. This technique reveals similar early aggregation steps but different later condensation pathways for various monoclonal antibodies.

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Last Updated: Jun 10, 2026

Visualization of Recombinant DNA and Protein Complexes Using Atomic Force Microscopy

Visualization of Recombinant DNA and Protein Complexes Using Atomic Force Microscopy

Published on: July 18, 2011

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

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Published on: July 10, 2019

Area of Science:

Biochemistry
Protein Science
Immunology

Background:

Therapeutic protein aggregation is a significant challenge in biopharmaceutical development.
Aggregation can lead to infusion reactions and clinical immunogenicity, impacting drug efficacy and safety.
Characterizing intermediate aggregation steps is crucial but technically demanding.

Purpose of the Study:

To investigate the morphology of monoclonal antibody aggregates using atomic force microscopy.
To elucidate the intermediate and subsequent stages of therapeutic protein aggregation.
To understand how antibody structure influences aggregation pathways.

Main Methods:

Atomic force microscopy (AFM) was employed to image monoclonal antibody aggregates at the molecular scale.
Biophysical methods were used to assess secondary and tertiary structures and size distribution.
Comparative analysis of different monoclonal antibodies with varying primary structures was performed.

Main Results:

Atomic force microscopy provided detailed insights into antibody aggregate morphology.
A common aggregation intermediate, comprising several monomers, was observed across different antibodies.
Subsequent condensation pathways of these oligomers varied among the antibodies studied, suggesting stability-dependent mechanisms.

Conclusions:

Atomic force microscopy is a valuable tool for characterizing protein aggregation intermediates.
Monoclonal antibody aggregation involves conserved early steps but divergent later condensation processes.
Antibody stability appears to be a key factor influencing aggregation mechanisms.