Tudor Luchian

TL;DR: It is demonstrated how peptide passage through the α-hemolysin protein can be sufficiently slowed down to observe intermediate single-peptide sub-states associated to distinct structural milestones along the pore, and how to control residence time, direction and the sequence of spatio-temporal state-to-state dynamics of a single peptide.

TL;DR: The kinetic analysis of a peptide fluctuating between various microstates inside the nanopore enabled a detailed picture of the free energy description of its interaction with the α-HL nanopore, and when studied at the limit of vanishingly low transmembrane potentials, this provided a thermodynamic description of peptide reversible binding to and within the β-barrel domain.

TL;DR: This work was supported by the Office of Naval Research, the U.S. Department of Energy, the Multidisciplinary University Research Initiative (ONR-1999), and the National Institutes of Health.

TL;DR: The use of the nanopore formed by Staphylococcus aureus α-hemolysin and polypeptides with oppositely charged segments at the N- and C-termini to increase both thepolypeptide capture rate and mean residence time of them in the pore, regardless of the polarity of the applied electrostatic potential is described.