title: Influence of Adsorption on Proteins and Amyloid Detection by Silicon Nitride Nanopore.
abstract: For the past 2 decades, emerging single-nanopore technologies have opened the route to multiple sensing applications. Besides DNA sensing, the identification of proteins and amyloids is a promising field for early diagnosis. However, the influence of the interactions between the nanopore surface and proteins should be taken into account. In this work, we have selected three proteins (avidin, lysozyme, and IgG) that exhibit different affinities with the SiNx surface, and we have also examined lysozyme amyloid. Our results show that the piranha treatment of SiNx significantly decreases protein adsorption. Moreover, we have successfully detected all proteins (pore diameter 17 nm) and shown the possibility of discriminating between denatured lysozyme and its amyloid. For all proteins, the capture rates are lower than expected, and we evidence that they are correlated with the affinity of proteins to the surface. Our result confirms that proteins interacting only with the nanopore surface wall stay long enough to be detected. For lysozyme amyloid, we show that the use of the nanopore is suitable for determining the number of monomer units even if only the proteins interacting with the nanopore are detected.
authors: Institut Européen des Membranes, UMR5635, Université de Montpellier CNRS ENSCM , Place Eugène Bataillon, 34095 Montpellier Cedex 5, France.
authors: Sébastien
authors: S
authors: Balme
authors: Laboratoire des Solides Irradiés, École polytechnique, Université Paris-Saclay , Route de Saclay, 91128 Palaiseau Cedex, France.
authors: Pierre Eugène
authors: PE
authors: Coulon
authors: Institut Européen des Membranes, UMR5635, Université de Montpellier CNRS ENSCM , Place Eugène Bataillon, 34095 Montpellier Cedex 5, France.
authors: Mathilde
authors: M
authors: Lepoitevin
authors: Institut d'Electronique et des Systèmes, Université de Montpellier , 34095 Montpellier Cedex 5, France.
authors: Benoît
authors: B
authors: Charlot
authors: Centre d'Études d'Agents Pathogènes et Biotechnologies pour la Santé (CPBS), CNRS UMR5236 , 34293 Montpellier, France.
authors: Naresh
authors: N
authors: Yandrapalli
authors: Centre d'Études d'Agents Pathogènes et Biotechnologies pour la Santé (CPBS), CNRS UMR5236 , 34293 Montpellier, France.
authors: Cyril
authors: C
authors: Favard
authors: Centre d'Études d'Agents Pathogènes et Biotechnologies pour la Santé (CPBS), CNRS UMR5236 , 34293 Montpellier, France.
authors: Delphine
authors: D
authors: Muriaux
authors: Institut Européen des Membranes, UMR5635, Université de Montpellier CNRS ENSCM , Place Eugène Bataillon, 34095 Montpellier Cedex 5, France.
authors: Mikhael
authors: M
authors: Bechelany
authors: Institut Européen des Membranes, UMR5635, Université de Montpellier CNRS ENSCM , Place Eugène Bataillon, 34095 Montpellier Cedex 5, France.
authors: Jean-Marc
authors: JM
authors: Janot
mesh_terms: D000327:Adsorption; D000682:Amyloid / Q000032:analysis* / Q000737:chemistry; D001360:Avidin / Q000032:analysis* / Q000737:chemistry; D055664:Electrochemical Techniques; D007074:Immunoglobulin G / Q000032:analysis* / Q000737:chemistry; D007700:Kinetics; D009113:Muramidase / Q000032:analysis* / Q000737:chemistry; D058608:Nanopores / Q000648:ultrastructure; D017655:Silicon Compounds / Q000737:chemistry*; D012996:Solutions
chemical_list: D000682:Amyloid; D007074:Immunoglobulin G; D017655:Silicon Compounds; D012996:Solutions; D001360:Avidin; D009113:Muramidase; C032734:silicon nitride