Force spectroscopy in studying infection

TL;DR

Force spectroscopy techniques like optical and atomic force microscopy provide detailed insights into the mechanical properties of biological specimens, aiding infection research and therapeutic development.

Contribution

This review highlights how force spectroscopy tools are tailored to study infection-related biological processes, offering unique insights beyond traditional ensemble methods.

Findings

Revealed mechanical properties of virus-cell interactions

Demonstrated the role of force spectroscopy in understanding protein processivity

Showcased applications in structure-based drug design

Abstract

Biophysical force spectroscopy tools - for example optical tweezers, magnetic tweezers, atomic force microscopy, - have been used to study elastic, mechanical, conformational and dynamic properties of single biological specimens from single proteins to whole cells to reveal information not accessible by ensemble average methods such as X-ray crystallography, mass spectroscopy, gel electrophoresis and so on. Here we review the application of these tools on a range of infection-related questions from antibody-inhibited protein processivity to virus-cell adhesion. In each case we focus on how the instrumental design tailored to the biological system in question translates into the functionality suitable for that particular study. The unique insights that force spectroscopy has gained to complement knowledge learned through population averaging techniques in interrogating biomolecular details prove to be instrumental in therapeutic innovations such as those in structure-based drug design.