A single biomolecule interface for advancing the sensitivity, selectivity and accuracy of sensors

Ying, Yi‐Lun; Cao, Chunhua; Hu, Yong‐Xu; Long, Yi‐Tao

doi:10.1093/nsr/nwy029

Cited by 66 publications

(61 citation statements)

References 10 publications

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“…11 In general, biological nanopores are superior in the sensing of oligonucleotides, peptides, organic molecules and other small molecules, but not proteins and other large sized entities, owing to the 1-2 nm narrowest part of the pore lumen. 12,13 Attributed to the size tunable features and easy fabrication process, glass nanopore sensors have broadened the application for single entity analysis. [14][15][16] Traditional glass nanopore sensors are mainly based on the volume exclusion mechanism, which can be briey described as the transient decrease of pore conductance resulting from the single entity traversing through the nanopore, exhibiting pulse like blockage signals on the ionic current.…”

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confidence: 99%

Single molecule sensing of amyloid-β aggregation by confined glass nanopores

et al. 2019

Chem. Sci.

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Single molecule sensing of amyloid-β aggregation by confined glass nanopores

et al. 2019

Chem. Sci.

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“…[6] Measuring such low fluxes is achallenge.Porins provide an anoscale confined space perfect for singlemolecule analysis. [7] Penetration and binding of the substrate lead to significant ion-current fluctuations.H owever,r ecognition and binding do not provide direct information on genuine translocation. [8] In the case of charged molecules,t he reversal potential may give ad irect information on the net flux.…”

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Small‐Molecule Permeation across Membrane Channels: Chemical Modification to Quantify Transport across OmpF

et al. 2019

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Biological channels facilitate the exchange of molecules across membranes,b ut general tools to quantify transport are missing. Electrophysiology is the method of choice to study the functional properties of channels.However, analyzing the current fluctuation of channelstypically does not identify successful transport, that is,d istinguishing translocation from binding.T odistinguish both processes,weadded an additional barrier at the channel exit acting as am olecular counter.T oi dentify permeation, we compare the molecule residence time in the native channel with one that is chemically modified at the exit. We use the well-studied outer membrane channel from E. coli, OmpF.P osition 181, whichi sb elowt he constriction region, was subsequently mutated into cysteine (E181C) in an otherwise cysteine-free system, then functionalized by covalent binding with one of the two blockers MTSES or GLT. We measured the passage of model peptides, mono-, tri-, hepta-arginine and of norfloxacin, as an example for antibiotic permeation.

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“…[27,28] The physical and chemical properties of the studied analyte including its size, concentration, conformation, structure, charge, and interaction with the pore can be inferred from statistical analysis of the blockade events. [29][30][31] The detection of peptides/proteins by the nanopore technique has become a research hotspot in recent years. Peptides or proteins are basic substances that make up cells, and play important roles in all aspects of life.…”

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Single‐Molecule Study of Peptides with the Same Amino Acid Composition but Different Sequences by Using an Aerolysin Nanopore

Angelov

et al. 2020

ChemBioChem

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Nanopores are original sensors employed for highly sensitive peptides/proteins detection. Herein, we describe the use of an aerolysin nanopore to identify two similar model peptides, YEQYEQQDDDRQQQ (YEQ2Q3) and QDDDRQQQYEQYEQ (Q3YEQ2), with the same amino acid composition but different sequences. All‐atom molecular dynamics (MD) simulations reveal that YEQ2Q3 possesses fewer hydrogen bonds and a more extended conformation than Q3YEQ2. These two peptides, which fold differently, exhibit obviously distinct mass‐independent current blockades with characteristic dwell times when entering the aerolysin nanopore. Typically, at +60 mV, the statistical dwell time of 0.630±0.018 ms for peptide Q3YEQ2 is four times longer than the value of 0.160±0.001 ms for peptide YEQ2Q3, and yet peptide YEQ2Q3 induces ∼1.9 % larger blockade current amplitude than peptide Q3YEQ2. The obtained results show the remarkable potential of aerolysin nanopore for peptides/proteins identification, characterization, sequencing and also demonstrate that the mass identification of nonuniformly charged peptides/proteins by using the nanopore technique could be complicated by their folded structure and complex analyte‐pore interaction.

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A single biomolecule interface for advancing the sensitivity, selectivity and accuracy of sensors

Cited by 66 publications

References 10 publications

Single molecule sensing of amyloid-β aggregation by confined glass nanopores

Single molecule sensing of amyloid-β aggregation by confined glass nanopores

Small‐Molecule Permeation across Membrane Channels: Chemical Modification to Quantify Transport across OmpF

Single‐Molecule Study of Peptides with the Same Amino Acid Composition but Different Sequences by Using an Aerolysin Nanopore

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