Despite success in probing chemical reactions and dynamics of macromolecules on submillisecond time and nanometer length scales, a major impasse faced by nanopore technology is the need to cheaply and controllably modulate macromolecule capture and trafficking across the nanopore. We demonstrate herein that tunable charge separation engineered at the both ends of a macromolecule very efficiently modulates the dynamics of macromolecules capture and traffic through a nanometer-size pore. In the proof-of-principle approach, we employed a 36 amino acids long peptide containing at the N- and C-termini uniform patches of glutamic acids and arginines, flanking a central segment of asparagines, and we studied its capture by the alpha-hemolysin (alpha-HL) and the mean residence time inside the pore in the presence of a pH gradient across the protein. We propose a solution to effectively control the dynamics of peptide interaction with the nanopore, with both association and dissociation reaction rates of peptide-alpha-HL interactions spanning orders of magnitude depending upon solution acidity on the peptide addition side and the transmembrane electric potential, while preserving the amplitude of the blockade current signature.

Asandei, A., Chinappi, M., Kang, H.-., Seo, C.h., Mereuta, L., Park, Y., et al. (2015). Acidity-Mediated, Electrostatic Tuning of Asymmetrically Charged Peptides Interactions with Protein Nanopores. ACS APPLIED MATERIALS & INTERFACES, 7(30), 16706-16714 [10.1021/acsami.5b04406].

Acidity-Mediated, Electrostatic Tuning of Asymmetrically Charged Peptides Interactions with Protein Nanopores

Chinappi M.;
2015-01-01

Abstract

Despite success in probing chemical reactions and dynamics of macromolecules on submillisecond time and nanometer length scales, a major impasse faced by nanopore technology is the need to cheaply and controllably modulate macromolecule capture and trafficking across the nanopore. We demonstrate herein that tunable charge separation engineered at the both ends of a macromolecule very efficiently modulates the dynamics of macromolecules capture and traffic through a nanometer-size pore. In the proof-of-principle approach, we employed a 36 amino acids long peptide containing at the N- and C-termini uniform patches of glutamic acids and arginines, flanking a central segment of asparagines, and we studied its capture by the alpha-hemolysin (alpha-HL) and the mean residence time inside the pore in the presence of a pH gradient across the protein. We propose a solution to effectively control the dynamics of peptide interaction with the nanopore, with both association and dissociation reaction rates of peptide-alpha-HL interactions spanning orders of magnitude depending upon solution acidity on the peptide addition side and the transmembrane electric potential, while preserving the amplitude of the blockade current signature.
2015
Pubblicato
Rilevanza internazionale
Articolo
Esperti anonimi
Settore ING-IND/34 - BIOINGEGNERIA INDUSTRIALE
Settore FIS/07 - FISICA APPLICATA (A BENI CULTURALI, AMBIENTALI, BIOLOGIA E MEDICINA)
English
Con Impact Factor ISI
protein nanopore; nanoscale peptide trafficking single-molecule eleetrophysiology; lipid bilayer interfaces; biotechnology; control of peptide dynamics
Asandei, A., Chinappi, M., Kang, H.-., Seo, C.h., Mereuta, L., Park, Y., et al. (2015). Acidity-Mediated, Electrostatic Tuning of Asymmetrically Charged Peptides Interactions with Protein Nanopores. ACS APPLIED MATERIALS & INTERFACES, 7(30), 16706-16714 [10.1021/acsami.5b04406].
Asandei, A; Chinappi, M; Kang, H-; Seo, Ch; Mereuta, L; Park, Y; Luchian, T
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/247515
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