ArticleBiophysical journal2014
Temperature and electrolyte optimization of the α-hemolysin latch sensing zone for detection of base modification in double-stranded DNA.
Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 23 citations in OpenAlex.
- Complex and Non-sequential Current Signatures of a β-Hairpin Peptide Confined in a Nanopore.Analytical chemistry · 2025Article
- Analytical and Structural Studies for the Investigation of Oxidative Stress in Guanine Oligonucleotides.International journal of molecular sciences · 2020Review
- Biomimetic Membranes with Transmembrane Proteins: State-of-the-Art in Transmembrane Protein Applications.International journal of molecular sciences · 2019Review
- Dynamics of a DNA Mismatch Site Held in Confinement Discriminate Epigenetic Modifications of Cytosine.Journal of the American Chemical Society · 2017Article
- Nanopore Sensing.Analytical chemistry · 2017Review
- Kinetics of T3-DNA Ligase-Catalyzed Phosphodiester Bond Formation Measured Using the α-Hemolysin Nanopore.ACS nano · 2016Article
- Energetics of base flipping at a DNA mismatch site confined at the latch constriction of α-hemolysin.Faraday discussions · 2016Article
- Hydroxymethyluracil modifications enhance the flexibility and hydrophilicity of double-stranded DNA.Nucleic acids research · 2016Article
- Base Flipping within the α-Hemolysin Latch Allows Single-Molecule Identification of Mismatches in DNA.Journal of the American Chemical Society · 2016Article
- Unzipping of A-Form DNA-RNA, A-Form DNA-PNA, and B-Form DNA-DNA in the α-Hemolysin Nanopore.Biophysical journal · 2016Article
- Differentiation of G:C vs A:T and G:C vs G:mC Base Pairs in the Latch Zone of α-Hemolysin.ACS nano · 2015Article
- Identification of DNA lesions using a third base pair for amplification and nanopore sequencing.Nature communications · 2015Article
- 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
- Biomedical diagnosis perspective of epigenetic detections using alpha-hemolysin nanopore.AIMS materials science · 2015Article
- Internal vs fishhook hairpin DNA: unzipping locations and mechanisms in the α-hemolysin nanopore.The journal of physical chemistry. B · 2014Article
- Effect of an Electrolyte Cation on Detecting DNA Damage with the Latch Constriction of α-Hemolysin.The journal of physical chemistry letters · 2014Article
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5 authors at 1 institution in 1 country.
Funding
Abstract
The latch region of the wild-type protein pore α-hemolysin (α-HL) constitutes a sensing zone for individual abasic sites (and furan analogs) in double-stranded DNA (dsDNA). The presence of an abasic site or furan within a DNA duplex, electrophoretically captured in the α-HL vestibule and positioned at the latch region, can be detected based on the current blockage prior to duplex unzipping. We investigated variations in blockage current as a function of temperature (12-35°C) and KCl concentration (0.15-1.0 M) to understand the origin of the current signature and to optimize conditions for identifying the base modification. In 1 M KCl solution, substitution of a furan for a cytosine base in the latch region results in an ∼ 8 kJ mol(-1) decrease in the activation energy for ion transport through the protein pore. This corresponds to a readily measured ∼ 2 pA increase in current at room temperature. Optimal resolution for detecting the presence of a furan in the latch region is achieved at lower KCl concentrations, where the noise in the measured blockage current is significantly lower. The noise associated with the blockage current also depends on the stability of the duplex (as measured from the melting temperature), where a greater noise in the measured blockage current is observed for less stable duplexes.
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