Influence of Adsorption on Proteins and Amyloid Detection by Silicon Nitride Nanopore

• Published in: Langmuir Vol. 32; no. 35; pp. 8916 - 8925
• Main Authors: Balme, Sébastien, Coulon, Pierre Eugène, Lepoitevin, Mathilde, Charlot, Benoît, Yandrapalli, Naresh, Favard, Cyril, Muriaux, Delphine, Bechelany, Mikhael, Janot, Jean-Marc
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 06.09.2016
• Subjects: Adsorption; Amyloid - analysis; Amyloid - chemistry; Avidin - analysis; Avidin - chemistry; Chemical Sciences; Electrochemical Techniques; Immunoglobulin G - analysis; Immunoglobulin G - chemistry; Interface Components: Nanops, Colloids, Emulsions, Surfactants, Proteins, Polymers; Kinetics; Muramidase - analysis; Muramidase - chemistry; Nanopores - ultrastructure; Silicon Compounds - chemistry; Solutions
• ISSN: 0743-7463; 1520-5827
• DOI: 10.1021/acs.langmuir.6b02048

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 SiN x surface, and we have also examined lysozyme amyloid. Our results show that the piranha treatment of SiN x 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.