Atomic Force Microscopy of Protein Shells: Virus Capsids and Beyond.

Area of Science:

• Biophysics
• Nanotechnology
• Materials Science

Background:

• Atomic Force Microscopy (AFM) utilizes a nanometric tip on a microcantilever to probe specimens.
• AFM enables high-resolution imaging of individual protein shells, like viruses, in liquid environments.

Purpose of the Study:

• To review methods for adsorbing protein shells onto surfaces for AFM analysis.
• To present various AFM approaches for studying protein cages, including imaging and spectroscopy.
• To extract physical information, such as mechanical and electrostatic properties, from single protein cages.

Main Methods:

• Surface adsorption techniques for protein shells.
• AFM imaging for nanometric resolution of protein structures in liquid.
• AFM-based spectroscopy for characterizing mechanical and electrostatic properties.

Main Results:

• Demonstration of AFM's capability for imaging individual protein shells at nanometric resolution.
• Successful application of AFM for manipulating single protein cages.
• Characterization of physicochemical properties of protein cages using AFM.

Conclusions:

• AFM is a versatile tool for both imaging and probing the physical properties of individual protein shells.
• The presented AFM methodologies provide valuable insights into the mechanics and electrostatics of protein cages.
• This work highlights AFM's potential in advancing the study of biological macromolecules.