Characterization of Recognition Events between Proteins on a Single Molecule Level with Atomic Force Microscopy

Abstract

The application of functional imaging tools and techniques on the molecular level enables investigators to characterize structures of biomolecules and interactions between biomolecules. The characterization of recognition events between biomolecules with atomic force microscopy (AFM) is a new methodology in biological research. Recent advances in the field of scanning probe microscopy especially atomic force microscopy have made it possible to discover the dynamic systems of molecular self-assembly and quantify the molecular forces between proteins. The interaction mechanisms between biomolecules were explored by many researchers to tackle broad-category initiatives of human diseases. This review overviews the advances in characterizing recognition events between proteins on the molecular level, specifically on antigen−antibody interactions and the aggregation of amyloid-β peptides. AFM as an emerging approach for characterizing biomolecular interactions will also be highlighted. Furthermore, the potential and limitations of AFM for the measurement of single molecule interactions and the issues in analysis procedure will be discussed.

Novel perspective for protein–drug interaction analysis: atomic force microscope

“…Recently, numerous reviews have been published that discuss AFM in further detail. [12][13][14][15] Investigation on drug effects can be performed by the most frequently used AFM operating modes, namely imaging and force spectroscopy modes.…”

Revealing the Effect of Photothermal Therapy on Human Breast Cancer Cells: A Combined Study from Mechanical Properties to Membrane HSP70

“…HSP70 consists of a C-terminal substrate-binding domain and an N-terminal nucleotide-binding domain, interconnected by a short, hydrophobic, and highly conserved chain . The extracellular motif TKDNNLLGRFELSG (TKD) of HSP70, located near the C-terminal substrate binding domain, has been proven to bind exclusively to aptamer A8 (Figure a). , AFM-based SMFS can directly measure the interaction between receptor–ligand, protein–protein, antigen–antibody, and other molecules . To acquire preliminary insight into aptamer A8 and HSP70 binding, we created a platform for analyzing aptamer A8 interaction with HSP70 by AFM-based SMFS.…”

Aptamer as a Tool for Investigating the Effects of Electric Field on Aβ40 Monomer and Aggregates Using Single-Molecule Force Spectroscopy

“…AFM-based single-molecule force spectroscopy (SMFS) has been highlighted for characterizing recognition events at the single-molecule level, although it is essential to use expensive and specialized equipment for SMFS experiments. Especially, it has opened new perspectives in exploring the intramolecular and intermolecular interactions because of its pico-Newton (pN) sensitivity and the capability of operating under different physiological conditions .…”

“…Additionally, the majority of the theoretical and experimental research focused on the effect of EF on folding and unfolding processes 18 of amyloid proteins (monomers) or dissociation and elimination of preformed amyloid fibrils. 19 AFM-based single-molecule force spectroscopy (SMFS) has been highlighted for characterizing recognition events at the single-molecule level, 20 although it is essential to use expensive and specialized equipment for SMFS experiments. Especially, it has opened new perspectives in exploring the intramolecular and intermolecular interactions because of its pico-Newton (pN) sensitivity and the capability of operating under different physiological conditions.…”