Electroosmotic flow through an 
                $$\alpha$$
                
                    
                                    
                        α
                    
                
            -hemolysin nanopore

Bonome, Emma Letizia; Cecconi, Fabio; Chinappi, Mauro

doi:10.1007/s10404-017-1928-1

Cited by 47 publications

(30 citation statements)

References 53 publications

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“…Molecular dynamics (MD) simulations have proved a useful computational tool to investigate transport phenomena in biological nanopore sensing systems and to interpret experimental data. Examples are the estimation of α-HL ionic conductance and electro-osmotic flow, [120,131,132] investigation of singlestranded DNA molecules inside α-HL, [133] the cotranslocational unfolding of thioredoxin, [134] and DNA base distinguishability in MspA. [135] A core question in nanopore protein sequencing is the capability to distinguish among the 20 amino acids.…”

Section: Insights On Protein Sequencing From Atomistic Simulationmentioning

confidence: 99%

“…[27,51,90,104,145,146] Our groups focused on a third strategy, namely adjusting the electro-osmotic flow (EOF). [69,132] EOF refers to the net motion of the solvent (usually water) induced by an applied voltage. If the nanopore is selective for cations (or anions), the positive and negative ion distributions inside the nanopore differ and, consequently, in some regions of the nanopore, the electrolyte solution presents an average net charge.…”

Section: Capture and Translocation Controlmentioning

confidence: 99%

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Nanopore‐Based Protein Sequencing Using Biopores: Current Achievements and Open Challenges

et al. 2020

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The synergy of life sciences discoveries, biomolecular and protein engineering advances, and groundbreaking nanofabrication technologies, has introduced over the past years the wide use of the nanopore-based investigations of matter at the molecular level. This review focuses on the fundamental principles of α-hemolysin (α-HL) protein-based nanopores, as sensitive investigative tools that combine single-molecule detection with the ability to simultaneously manipulate single molecules, in otherwise complex samples. Herein, there are presented some of the efforts directed to control the capture dynamics and translocation speed of tailored polypeptides through the α-HL nanopore, by harnessing the electro-osmotic flow and nanopore-tweezing influence on individual molecules, which are engineered to resemble macrodipoles. The reported applications of this approach suggest a solution to enhance the temporal resolution of nanopore detection, prove the capability of the system in distinguishing between groups of distinct amino acids from the studied poly peptides, and propose a strategy to translate such single-molecule sensors in devices suitable for polypeptide sequencing at unimolecular level.

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Section: Insights On Protein Sequencing From Atomistic Simulationmentioning

confidence: 99%

Section: Capture and Translocation Controlmentioning

confidence: 99%

Nanopore‐Based Protein Sequencing Using Biopores: Current Achievements and Open Challenges

et al. 2020

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“…Protein translocation speed can be slowed down by changing buffer conditions such as pH, or modifying the surface of pore to enhance the interaction between proteins and nanopore [46,77]. For both biological nanopores and solid-state nanopores [58,[115][116][117], pH changes have a relevant effect on electroosmotic flow that refers to the net motion of the solvent induced by an applied voltage. The interplay between electrophoresis and electroosmosis can modulate the passage of a peptide.…”

Section: Protein Sequencing Using Solid-state Nanoporesmentioning

confidence: 99%

“…The interplay between electrophoresis and electroosmosis can modulate the passage of a peptide. For a specific case of α-HL, low pH value increases its anion selectivity, leading to a corresponding increase in the electroosmotic speed of water against electrophoresis and thus reducing the net drift speed of the peptide [115][116][117]. Hu et al provided a novel approach.…”

Section: Protein Sequencing Using Solid-state Nanoporesmentioning

confidence: 99%

Application of Solid-State Nanopore in Protein Detection

Luo

et al. 2020

IJMS

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A protein is a kind of major biomacromolecule of life. Its sequence, structure, and content in organisms contains quite important information for normal or pathological physiological process. However, research of proteomics is facing certain obstacles. Only a few technologies are available for protein analysis, and their application is limited by chemical modification or the need for a large amount of sample. Solid-state nanopore overcomes some shortcomings of the existing technology, and has the ability to detect proteins at a single-molecule level, with its high sensitivity and robustness of device. Many works on detection of protein molecules and discriminating structure have been carried out in recent years. Single-molecule protein sequencing techniques based on solid-state nanopore are also been proposed and developed. Here, we categorize and describe these efforts and progress, as well as discuss their advantages and drawbacks.

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“…iv) The electroosmotic (elo) flow favors peptide capture at negative potentials present on the peptide addition side. In such cases and judged from the peptide addition side perspective, the elo flow through the slightly anionic selective α−HL is directed toward the nanopore entry [33,43,52]. This implies that for the trans-added peptides, electroosmosis favors the capture at negative ΔV's (i.e.…”

Section: The Case Of Peptide Association To the Nanoporementioning

confidence: 99%

Single-Molecule Dynamics and Discrimination between Hydrophilic and Hydrophobic Amino Acids in Peptides, through Controllable, Stepwise Translocation across Nanopores<strong> </strong>

Asandei

Dragomir

Muccio

et al. 2018

Preprint

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In this work we demonstrate the proof-of-concept of real-time discrimination between patches of serine or isoleucine monomers in the primary structure of custom-engineered, macrodipole-like peptides, at uni-molecular level. We employed single-molecule recordings to examine the ionic current through the α-hemolysin (α-HL) nanopore, when hydrophilic serine or hydrophobic isoleucine residues, flanked by segments of oppositely charged arginine and glutamic amino acids functioning as a voltage-dependent 'molecular brake' on the peptide, were driven at controllable rates across the nanopore. The observed differences in the ionic currents blockades through the nanopore, visible at time resolutions corresponding to peptide threading through the α-HL's constriction region, was explained by a simple model of the volumes of electrolyte excluded by either amino acid species, as groups of three serine or isoleucine monomers transiently occupy the α-HL. To provide insights into the conditions ensuring optimal throughput of peptide readout through the nanopore, we probed the sidedness-dependence of peptide association to and dissociation from the electrically and geometrically asymmetric α-HL.

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Electroosmotic flow through an $$\alpha$$ α -hemolysin nanopore

Cited by 47 publications

References 53 publications

Nanopore‐Based Protein Sequencing Using Biopores: Current Achievements and Open Challenges

Nanopore‐Based Protein Sequencing Using Biopores: Current Achievements and Open Challenges

Application of Solid-State Nanopore in Protein Detection

Single-Molecule Dynamics and Discrimination between Hydrophilic and Hydrophobic Amino Acids in Peptides, through Controllable, Stepwise Translocation across Nanopores<strong> </strong>

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