Setting Up a Bio-AFM to Study Protein Misfolding in Neurodegenerative Diseases

Dionysios Cheirdaris; Marios G Krokidis; Marianne Kasti; Aristidis G Vrahatis; Themistoklis Exarchos; Panagiotis Vlamos

doi:10.1007/978-3-031-31978-5_1

Setting Up a Bio-AFM to Study Protein Misfolding in Neurodegenerative Diseases

Adv Exp Med Biol. 2023:1423:1-10. doi: 10.1007/978-3-031-31978-5_1.

Authors

Dionysios Cheirdaris¹, Marios G Krokidis¹, Marianne Kasti¹, Aristidis G Vrahatis¹, Themistoklis Exarchos¹, Panagiotis Vlamos¹

Affiliation

¹ Bioinformatics and Human Electrophysiology Laboratory, Department of Informatics, Ionian University, Corfu, Greece.

PMID: 37525028
DOI: 10.1007/978-3-031-31978-5_1

Abstract

The clinical pathology of neurodegenerative diseases suggests that earlier onset and progression are related to the accumulation of protein aggregates due to misfolding. A prominent way to extract useful information regarding single-molecule studies of protein misfolding at the nanoscale is by capturing the unbinding molecular forces through forced mechanical tension generated and monitored by an atomic force microscopy-based single-molecule force spectroscopy (AFM-SMFS). This AFM-driven process results in an amount of data in the form of force versus molecular extension plots (force-distance curves), the statistical analysis of which can provide insights into the underlying energy landscape and assess a number of characteristic elastic and kinetic molecular parameters of the investigated sample. This chapter outlines the setup of a bio-AFM-based SMFS technique for single-molecule probing. The infrastructure used as a reference for this presentation is the Bruker ForceRobot300.

Keywords: Atomic force microscopy; Force-distance curves; Protein probing; Single molecule force spectroscopy.

MeSH terms

Humans
Microscopy, Atomic Force / methods
Nanotechnology
Neurodegenerative Diseases*
Proteins / chemistry
Single Molecule Imaging

Substances

Proteins