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Journal ArticleDOI

Multiparametric imaging of biological systems by force-distance curve-based AFM.

TLDR
The principles and applications of advanced FD-based AFM tools for the quantitative multiparametric characterization of complex cellular and biomolecular systems under physiological conditions are discussed.
Abstract
A current challenge in the life sciences is to understand how biological systems change their structural, biophysical and chemical properties to adjust functionality. Addressing this issue has been severely hampered by the lack of methods capable of imaging biosystems at high resolution while simultaneously mapping their multiple properties. Recent developments in force-distance (FD) curve–based atomic force microscopy (AFM) now enable researchers to combine (sub)molecular imaging with quantitative mapping of physical, chemical and biological interactions. Here we discuss the principles and applications of advanced FD-based AFM tools for the quantitative multiparametric characterization of complex cellular and biomolecular systems under physiological conditions.

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Citations
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Journal ArticleDOI

Imaging modes of atomic force microscopy for application in molecular and cell biology

TL;DR: The basic principles, advantages and limitations of the most common AFM bioimaging modes are reviewed, including the popular contact and dynamic modes, as well as recently developed modes such as multiparametric, molecular recognition, multifrequency and high-speed imaging.
Journal ArticleDOI

Atomic force microscopy-based mechanobiology

TL;DR: The potential of combining AFM with complementary techniques, including optical microscopy and spectroscopy of mechanosensitive fluorescent constructs, super-resolution microscopy, the patch clamp technique and the use of microstructured and fluidic devices to characterize the 3D distribution of mechanical responses within biological systems and to track their morphology and functional state as discussed by the authors.
Journal ArticleDOI

Bacterial adhesion at the single-cell level

TL;DR: Understanding of the mechanisms governing bacterial adhesion at the single-cell level is summarized, including the physical forces experienced by a cell before reaching the surface, the first contact with a surface and the transition from reversible to permanent adhesion.
References
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Journal ArticleDOI

Nanotomography with enhanced resolution using bimodal atomic force microscopy

TL;DR: In this article, high resolution volume images of semicrystalline polypropylene were obtained by stepwise wet-chemical etching followed by atomic force microscopy of the specimen.
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Nanomechanical properties of proteins and membranes depend on loading rate and electrostatic interactions.

TL;DR: The viscoelastic properties of the native light-driven proton pump bacteriorhodopsin of the purple membrane of Halobacterium salinarum are characterized and indicate that the mechanical response of membranes and proteins and probably of other biomolecular systems should be determined at different loading rates to fully understand their properties.
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Material Properties of Lipid Microdomains: Force-Volume Imaging Study of the Effect of Cholesterol on Lipid Microdomain Rigidity

TL;DR: The results can lead to a better understanding of the role that CHOL plays in the mechanical properties of cellular membranes in modulating membrane rigidity, which has important implications for cellular mechanotransduction.
Journal ArticleDOI

Quantification of the number of EP3 receptors on a living CHO cell surface by the AFM.

TL;DR: The result indicated that the number of receptors on a living cell surface could be quantified through the force measurement by the AFM, and it was unlikely that the receptors were extracted from the cell membrane during the experiments.
Journal ArticleDOI

Out but Not In: The Large Transmembrane β-Barrel Protein FhuA Unfolds but Cannot Refold via β-Hairpins

TL;DR: Single-molecule force spectroscopy is used to characterize the un- and refolding of the ferric hydroxamate uptake receptor (FhuA), which is one of the largest β-barrel proteins of the outer membrane of Escherichia coli, and suggests that large β- barrel proteins that show more complex (un-)folding pathways require cofactors for proper insertion and folding into the membrane.
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