Measuring Force-Induced Dissociation Kinetics of Protein Complexes Using Single-Molecule Atomic Force Microscopy

Manibog, Kristine; Yen, Chi-Fu; Sivasankar, Sanjeevi

doi:10.1016/bs.mie.2016.08.009

Cited by 8 publications

(7 citation statements)

References 65 publications

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“…As a result, the FNA is anchored between the tip and the surface; therefore, the interaction between the monomers of the trimer is probed during the retraction step. Biotin–streptavidin is a robust and stable complex that requires a large force for its rupture and is used in numerous force spectroscopy experiments that utilize AFM force spectroscopy, , optical , and magnetic tweezers, and single-molecule fluorescence spectroscopy. , Notably, the unbinding peak for this complex plays a role of the internal reference used for characterizing other peaks that correspond to peptide–peptide interactions. To assign peaks for biotin–streptavidin complexes in force–distance (FD) curves, control experiments with the FNA containing no peptides were performed (Supporting Information, Figure S3).…”

Section: Resultsmentioning

confidence: 99%

Probing Intermolecular Interactions within the Amyloid β Trimer Using a Tethered Polymer Nanoarray

2018

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Amyloid oligomers are considered the most neurotoxic species of amyloid aggregates. Spontaneous assembly of amyloids into aggregates is recognized as a major molecular mechanism behind Alzheimer's disease and other neurodegenerative disorders involving protein aggregation. Characterization of such oligomers is extremely challenging but complicated by their transient nature. Previously, we introduced a flexible nanoarray (FNA) method enabling us to probe dimers assembled by the amyloid β (14-23) [Aβ (14-23)] peptide. The study presented herein modifies and enhances this approach to assemble and probe trimers of Aβ (14-23). A metal-free click chemistry approach was used, in which dibenzocyclooctyne (DBCO) groups were incorporated at selected sites within the FNA template to click Aβ (14-23) monomers at their terminal azide groups. Atomic force microscopy (AFM) force spectroscopy was employed to characterize the assemblies. The force measurement data demonstrate that the dissociation of the trimer undergoes a stepwise pattern, in which the first monomer dissociates at the rupture force ∼48 ± 2.4 pN. The remaining dimer ruptures at the second step at a slightly larger rupture force (∼53 ± 3.2 pN). The assembled trimer was found to be quite dynamic, and transient species of this inherently dynamic process were identified.

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Section: Resultsmentioning

confidence: 99%

Probing Intermolecular Interactions within the Amyloid β Trimer Using a Tethered Polymer Nanoarray

2018

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“…Force controlled methods provide a direct determination of force-related probabilities of these processes. Force clamp AFM studies have also demonstrated the existence of catch bonds [33], a type of noncovalent bond that resist dissociation when tensile force increases [34].…”

Section: Atomic Force Microscopy As a Direct Force-probing Techniquementioning

confidence: 99%

Quantifying molecular- to cellular-level forces in living cells

Pan¹,

Kmieciak²,

Liu³

et al. 2021

J. Phys. D: Appl. Phys.

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Mechanical cues have been suggested to play an important role in cell functions and cell fate determination, however, such physical quantities are challenging to directly measure in living cells with single molecule sensitivity and resolution. In this review, we focus on two main technologies that are promising in probing forces at the single molecule level. We review their theoretical fundamentals, recent technical advancements, and future directions, tailored specifically for interrogating mechanosensitive molecules in live cells.

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“…Protein-protein unbinding kinetics can alternatively be measured as a function of time using a constant pulling force (or force clamp). This approach has not been used on food systems (Manibog, Yen, & Sivasankar, 2017). In other cases, the AFM tip was functionalized with methyls, hydroxyls or other groups to measure the adhesion of proteins (Fahs & Louarn, 2013), bacteria (Dorobantu, Bhattacharjee, Foght, & Gray, 2008) or Saccharomyces cerevisiae yeast (Ahimou, Denis, Touhami, & Dufrene, 2002) to hydrophilic or hydrophobic surfaces.…”

Section: Adhesionmentioning

confidence: 99%

Atomic force microscopy of food assembly: Structural and mechanical insights at the nanoscale and potential opportunities from other fields

Obeid

Guyomarc’H

2020

Food Bioscience

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Measuring Force-Induced Dissociation Kinetics of Protein Complexes Using Single-Molecule Atomic Force Microscopy

Cited by 8 publications

References 65 publications

Probing Intermolecular Interactions within the Amyloid β Trimer Using a Tethered Polymer Nanoarray

Probing Intermolecular Interactions within the Amyloid β Trimer Using a Tethered Polymer Nanoarray

Quantifying molecular- to cellular-level forces in living cells

Atomic force microscopy of food assembly: Structural and mechanical insights at the nanoscale and potential opportunities from other fields

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