Discriminating short-range from van der Waals forces using total force data in noncontact atomic force microscopy

2014 ◽  
Vol 89 (23) ◽  
Author(s):  
Stefan Kuhn ◽  
Philipp Rahe
Keyword(s):  
Atomic Force Microscopy ◽  
Short Range ◽  
Van Der Waals ◽  
Van Der Waals Forces ◽  
Total Force ◽  
Force Microscopy ◽  
Atomic Force ◽  
Force Data

Corrections to the van der Waals forces in application to atomic force microscopy

1995 ◽  
Vol 328 (1-2) ◽  
pp. 129-134 ◽  
Author(s):  
M. Bordag ◽  
G.L. Klimchitskaya ◽  
V.M. Mostepanenko
Keyword(s):  
Atomic Force Microscopy ◽  
Van Der Waals ◽  
Van Der Waals Forces ◽  
Force Microscopy ◽  
Atomic Force

scholarly journals CO Tip Functionalization Inverts Atomic Force Microscopy Contrast via Short-Range Electrostatic Forces

2014 ◽  
Vol 112 (16) ◽  
Author(s):  
Maximilian Schneiderbauer ◽  
Matthias Emmrich ◽  
Alfred J. Weymouth ◽  
Franz J. Giessibl
Keyword(s):  
Atomic Force Microscopy ◽  
Short Range ◽  
Electrostatic Forces ◽  
Force Microscopy ◽  
Atomic Force

scholarly journals Bioconjugation Strategies for Connecting Proteins to DNA-Linkers for Single-Molecule Force-Based Experiments

Nanomaterials ◽  
2021 ◽  
Vol 11 (9) ◽  
pp. 2424
Author(s):  
Lyan M. van der Sleen ◽  
Katarzyna M. Tych
Keyword(s):  
Mechanical Properties ◽  
Atomic Force Microscopy ◽  
Optical Tweezers ◽  
Single Molecule ◽  
Short Range ◽  
Force Spectroscopy ◽  
Magnetic Tweezers ◽  
Single Molecule Force Spectroscopy ◽  
Force Microscopy ◽  
Atomic Force

The mechanical properties of proteins can be studied with single molecule force spectroscopy (SMFS) using optical tweezers, atomic force microscopy and magnetic tweezers. It is common to utilize a flexible linker between the protein and trapped probe to exclude short-range interactions in SMFS experiments. One of the most prevalent linkers is DNA due to its well-defined properties, although attachment strategies between the DNA linker and protein or probe may vary. We will therefore provide a general overview of the currently existing non-covalent and covalent bioconjugation strategies to site-specifically conjugate DNA-linkers to the protein of interest. In the search for a standardized conjugation strategy, considerations include their mechanical properties in the context of SMFS, feasibility of site-directed labeling, labeling efficiency, and costs.

scholarly journals Statistical Analysis of Long- and Short-Range Forces Involved in Bacterial Adhesion to Substratum Surfaces as Measured Using Atomic Force Microscopy

2011 ◽  
Vol 77 (15) ◽  
pp. 5065-5070 ◽  
Author(s):  
Yun Chen ◽  
Henk J. Busscher ◽  
Henny C. van der Mei ◽  
Willem Norde
Keyword(s):  
Atomic Force Microscopy ◽  
Cell Surface ◽  
Bacterial Adhesion ◽  
Short Range ◽  
Surface Site ◽  
Adhesion Forces ◽  
Acid Base ◽  
Force Microscopy ◽  
Atomic Force ◽  
Retraction Force

ABSTRACTSurface thermodynamic analyses of microbial adhesion using measured contact angles on solid substrata and microbial cell surfaces are widely employed to determine the nature of the adhesion forces, i.e., the interplay between Lifshitz-van der Waals and acid-base forces. While surface thermodynamic analyses are often viewed critically, atomic force microscopy (AFM) can also provide information on the nature of the adhesion forces by means of Poisson analysis of the measured forces. This review first presents a description of Poisson analysis and its underlying assumptions. The data available from the literature for different combinations of bacterial strains and substrata are then summarized, leading to the conclusion that bacterial adhesion to surfaces is generally dominated by short-range, attractive acid-base interactions, in combination with long-range, weaker Lifshitz-van der Waals forces. This is in line with the findings of surface thermodynamic analyses of bacterial adhesion. Comparison with single-molecule ligand-receptor forces from the literature suggests that the short-range-force contribution from Poisson analysis involves a discrete adhesive bacterial cell surface site rather than a single molecular force. The adhesion force arising from these cell surface sites and the number of sites available may differ from strain to strain. Force spectroscopy, however, involves the tedious task of identifying the minor peaks in the AFM retraction force-distance curve. This step can be avoided by carrying out Poisson analysis on the work of adhesion, which can also be derived from retraction force-distance curves. This newly proposed way of performing Poisson analysis confirms that multiple molecular bonds, rather than a single molecular bond, contribute to a discrete adhesive bacterial cell surface site.

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