Protein transport through a narrow solid-state nanopore at high voltage: experiments and theory

B Cressiot, A Oukhaled, G Patriarche… - ACS …, 2012 - ACS Publications
We report experimentally the transport of an unfolded protein through a narrow solid-state
nanopore of 3 nm diameter as a function of applied voltage. The random coil polypeptide …

Nanopore analysis: An emerging technique for studying the folding and misfolding of proteins

CA Madampage, O Tavassoly, C Christensen… - Prion, 2012 - Taylor & Francis
Nanopore analysis is an emerging technique that enables the investigation of the
conformation of a single peptide or protein molecule. Briefly, a pore is inserted into a …

Detection of peptides with different charges and lengths by using the aerolysin nanopore

S Li, C Cao, J Yang, YT Long - ChemElectroChem, 2019 - Wiley Online Library
The aerolysin nanopore has a high sensitivity for molecular sensing, owing to its super
narrow diameter and highly charged lumen structure. Here, taking advantages of its high …

Focus on protein unfolding through nanopores

B Cressiot, A Oukhaled, L Bacri, J Pelta - BioNanoScience, 2014 - Springer
In this review, we focus only on the unfolding of proteins through nanopores. We introduce
the principle of electrical detection with nanopores and how this technique provides …

Thermostable virus portal proteins as reprogrammable adapters for solid-state nanopore sensors

B Cressiot, SJ Greive, M Mojtabavi, AA Antson… - Nature …, 2018 - nature.com
Nanopore-based sensors are advancing the sensitivity and selectivity of single-molecule
detection in molecular medicine and biotechnology. Current electrical sensing devices are …

Dynamics and energy contributions for transport of unfolded pertactin through a protein nanopore

B Cressiot, E Braselmann, A Oukhaled, AH Elcock… - ACS …, 2015 - ACS Publications
To evaluate the physical parameters governing translocation of an unfolded protein across a
lipid bilayer, we studied protein transport through aerolysin, a passive protein channel, at the …

Pulling Peptides across Nanochannels: Resolving Peptide Binding and Translocation through the Hetero-oligomeric Channel from Nocardia farcinica

PR Singh, I Bárcena-Uribarri, N Modi… - ACS …, 2012 - ACS Publications
We investigated translocation of cationic peptides through nanochannels derived from the
Gram-positive bacterium Nocardia farcinica at the single-molecule level. The two subunits …

Cu (II) and dopamine bind to αsynuclein and cause large conformational changes

O Tavassoly, S Nokhrin, OY Dmitriev… - The FEBS …, 2014 - Wiley Online Library
αSynuclein (AS) is an intrinsically disordered protein that can misfold and aggregate to
form Lewy bodies in dopaminergic neurons, a classic hallmark of Parkinson's disease. The …

[HTML][HTML] Methamphetamine binds to α-synuclein and causes a conformational change which can be detected by nanopore analysis

O Tavassoly, JS Lee - FEBS letters, 2012 - Elsevier
α-Synuclein is an intrinsically disordered protein of 140 amino acids which is abundant in
dopaminergic neurons. Misfolding and aggregation of α-synuclein leads to the formation of …

The use of nanopore analysis for discovering drugs which bind to α-synuclein for treatment of Parkinson's disease

O Tavassoly, J Kakish, S Nokhrin, O Dmitriev… - European journal of …, 2014 - Elsevier
A major feature of Parkinson's disease is the formation of Lewy bodies in dopaminergic
neurons which consist of misfolded α-synuclein. The binding of natural products to α …