ArticleBiophysical journal2013
Nanopore force spectroscopy of aptamer-ligand complexes.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 25 citations in OpenAlex.
- Biological Nanopores: Engineering on Demand.Life (Basel, Switzerland) · 2021Review
- Sensing with Nanopores and Aptamers: A Way Forward.Sensors (Basel, Switzerland) · 2020Review
- Unfolding Kinetics of the Human Telomere i-Motif Under a 10 pN Force Imposed by the α-Hemolysin Nanopore Identify Transient Folded-State Lifetimes at Physiological pH.Journal of the American Chemical Society · 2015Article
- Nanopore sensing of individual transcription factors bound to DNA.Scientific reports · 2015Article
- Article
- Nanopores suggest a negligible influence of CpG methylation on nucleosome packaging and stability.Nano letters · 2015Article
- Detection of two isomeric binding configurations in a protein-aptamer complex with a biological nanopore.ACS nano · 2014Article
- Article
- Rationally manipulating aptamer binding affinities in a stem-loop molecular beacon.Bioconjugate chemistry · 2014Article
- Single-molecule investigation of G-quadruplex folds of the human telomere sequence in a protein nanocavity.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The stability of aptamer-ligand complexes is probed in nanopore-based dynamic force spectroscopy experiments. Specifically, the ATP-binding aptamer is investigated using a backward translocation technique, in which the molecules are initially pulled through an α-hemolysin nanopore from the cis to the trans side of a lipid bilayer membrane, allowed to refold and interact with their target, and then translocated back in the trans-cis direction. From these experiments, the distribution of bound and unbound complexes is determined, which in turn allows determination of the dissociation constant Kd ≈ 0.1 mM of the aptamer and of voltage-dependent unfolding rates. The experiments also reveal differences in binding of the aptamer to AMP, ADP, or ATP ligands. Investigation of an aptamer variant with a stabilized ATP-binding site indicates fast conformational switching of the original aptamer before ATP binding. Nanopore force spectroscopy is also used to study binding of the thrombin-binding aptamer to its target. To detect aptamer-target interactions in this case, the stability of the ligand-free aptamer-containing G-quadruplexes-is tuned via the potassium content of the buffer. Although the presence of thrombin was detected, limitations of the method for aptamers with strong secondary structures and complexes with nanomolar Kd were identified.
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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.