ArticleBiophysical journal2008
Effects of multiple-bond ruptures on kinetic parameters extracted from force spectroscopy measurements: revisiting biotin-streptavidin interactions.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 70 citations in OpenAlex.
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- Next Generation Methods for Single-Molecule Force Spectroscopy on Polyproteins and Receptor-Ligand Complexes.Frontiers in molecular biosciences · 2020Review
- Direction Matters: Monovalent Streptavidin/Biotin Complex under Load.Nano letters · 2019Article
- Force Spectroscopy Shows Dynamic Binding of Influenza Hemagglutinin and Neuraminidase to Sialic Acid.Biophysical journal · 2019Article
- How Do We Know when Single-Molecule Force Spectroscopy Really Tests Single Bonds?Biophysical journal · 2018Review
- Direct Reading of Bona Fide Barcode Assays for Diagnostics with Smartphone Apps.Scientific reports · 2015Article
- pH-dependent deformations of the energy landscape of avidin-like proteins investigated by single molecule force spectroscopy.Molecules (Basel, Switzerland) · 2014Article
- Cytoadherence of erythrocytes invaded by Plasmodium falciparum: quantitative contact-probing of a human malaria receptor.Acta biomaterialia · 2013Article
- A simple bioconjugate attachment protocol for use in single molecule force spectroscopy experiments based on mixed self-assembled monolayers.International journal of molecular sciences · 2012Article
- Rupture of multiple receptor-ligand bonds: bimodal distribution of bond rupture force.The European physical journal. E, Soft matter · 2012Article
- Adhesion of mussel foot protein Mefp-5 to mica: an underwater superglue.Biochemistry · 2012Article
- Long lifetime of hydrogen-bonded DNA basepairs by force spectroscopy.Biophysical journal · 2012Article
- Hidden multiple bond effects in dynamic force spectroscopy.Biophysical journal · 2012Article
- Force measurement enabling precise analysis by dynamic force spectroscopy.International journal of molecular sciences · 2012Article
- Article
- Kinetics of the multistep rupture of fibrin 'A-a' polymerization interactions measured using atomic force microscopy.Biophysical journal · 2009Article
- Discovery through the computational microscope.Structure (London, England : 1993) · 2009Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Force spectroscopy measurements of the rupture of the molecular bond between biotin and streptavidin often results in a wide distribution of rupture forces. We attribute the long tail of high rupture forces to the nearly simultaneous rupture of more than one molecular bond. To decrease the number of possible bonds, we employed hydrophilic polymeric tethers to attach biotin molecules to the atomic force microscope probe. It is shown that the measured distributions of rupture forces still contain high forces that cannot be described by the forced dissociation from a deep potential well. We employed a recently developed analytical model of simultaneous rupture of two bonds connected by polymer tethers with uneven length to fit the measured distributions. The resulting kinetic parameters agree with the energy landscape predicted by molecular dynamics simulations. It is demonstrated that when more than one molecular bond might rupture during the pulling measurements there is a noise-limited range of probe velocities where the kinetic parameters measured by force spectroscopy correspond to the true energy landscape. Outside this range of velocities, the kinetic parameters extracted by using the standard most probable force approach might be interpreted as artificial energy barriers that are not present in the actual energy landscape. Factors that affect the range of useful velocities are discussed.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.