Influence of Adsorption on Proteins and Amyloid Detection by Silicon Nitride Nanopore
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...
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Veröffentlicht in: | Langmuir 2016-09, Vol.32 (35), p.8916-8925 |
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creator | Balme, Sébastien Coulon, Pierre Eugène Lepoitevin, Mathilde Charlot, Benoît Yandrapalli, Naresh Favard, Cyril Muriaux, Delphine Bechelany, Mikhael Janot, Jean-Marc |
description | 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. |
doi_str_mv | 10.1021/acs.langmuir.6b02048 |
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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.</description><identifier>ISSN: 0743-7463</identifier><identifier>EISSN: 1520-5827</identifier><identifier>DOI: 10.1021/acs.langmuir.6b02048</identifier><identifier>PMID: 27506271</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>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</subject><ispartof>Langmuir, 2016-09, Vol.32 (35), p.8916-8925</ispartof><rights>Copyright © 2016 American Chemical Society</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a448t-41e41430abfdcfcbea60168ed2a2ef08f150037d7eb06970ed3bb6c74cbbeb493</citedby><cites>FETCH-LOGICAL-a448t-41e41430abfdcfcbea60168ed2a2ef08f150037d7eb06970ed3bb6c74cbbeb493</cites><orcidid>0000-0003-0244-9939 ; 0000-0003-0779-3384 ; 0000-0002-0663-2995 ; 0000-0002-8304-2980 ; 0000-0002-2913-2846 ; 0000-0001-7178-1949 ; 0000-0001-8631-5334 ; 0000-0001-8517-9342</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/acs.langmuir.6b02048$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/acs.langmuir.6b02048$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>230,314,780,784,885,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27506271$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.umontpellier.fr/hal-01681403$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Balme, Sébastien</creatorcontrib><creatorcontrib>Coulon, Pierre Eugène</creatorcontrib><creatorcontrib>Lepoitevin, Mathilde</creatorcontrib><creatorcontrib>Charlot, Benoît</creatorcontrib><creatorcontrib>Yandrapalli, Naresh</creatorcontrib><creatorcontrib>Favard, Cyril</creatorcontrib><creatorcontrib>Muriaux, Delphine</creatorcontrib><creatorcontrib>Bechelany, Mikhael</creatorcontrib><creatorcontrib>Janot, Jean-Marc</creatorcontrib><title>Influence of Adsorption on Proteins and Amyloid Detection by Silicon Nitride Nanopore</title><title>Langmuir</title><addtitle>Langmuir</addtitle><description>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.</description><subject>Adsorption</subject><subject>Amyloid - analysis</subject><subject>Amyloid - chemistry</subject><subject>Avidin - analysis</subject><subject>Avidin - chemistry</subject><subject>Chemical Sciences</subject><subject>Electrochemical Techniques</subject><subject>Immunoglobulin G - analysis</subject><subject>Immunoglobulin G - chemistry</subject><subject>Interface Components: Nanops, Colloids, Emulsions, Surfactants, Proteins, Polymers</subject><subject>Kinetics</subject><subject>Muramidase - analysis</subject><subject>Muramidase - chemistry</subject><subject>Nanopores - ultrastructure</subject><subject>Silicon Compounds - chemistry</subject><subject>Solutions</subject><issn>0743-7463</issn><issn>1520-5827</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kF1LwzAUhoMobn78A5Fe6kXnSZs23eXwa8JQQXcd8nGqkbaZSSvs35u56aVwIIfwvO-Bh5AzChMKGb2SOkwa2b21g_WTUkEGrNojY1pkkBZVxvfJGDjLU87KfESOQvgAgGnOpodklPECyozTMVk-dHUzYKcxcXUyM8H5VW9dl8R59q5H24VEdiaZtevGWZPcYI_6h1Dr5MU2Vsf10fbeGkweZedWzuMJOahlE_B09x6T5d3t6_U8XTzdP1zPFqlkrOpTRpFRloNUtdG1VihLoGWFJpMZ1lDVtADIueGooJxyQJMrVWrOtFKo2DQ_Jpfb3nfZiJW3rfRr4aQV89lCbP42dZRB_kUje7FlV959Dhh60dqgsYkO0Q1B0IryoigLXkWUbVHtXQge679uCmIjX0T54le-2MmPsfPdhUG1aP5Cv7YjAFtgE_9wg--inP87vwGAcZRE</recordid><startdate>20160906</startdate><enddate>20160906</enddate><creator>Balme, Sébastien</creator><creator>Coulon, Pierre Eugène</creator><creator>Lepoitevin, Mathilde</creator><creator>Charlot, Benoît</creator><creator>Yandrapalli, Naresh</creator><creator>Favard, Cyril</creator><creator>Muriaux, Delphine</creator><creator>Bechelany, Mikhael</creator><creator>Janot, Jean-Marc</creator><general>American Chemical Society</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0003-0244-9939</orcidid><orcidid>https://orcid.org/0000-0003-0779-3384</orcidid><orcidid>https://orcid.org/0000-0002-0663-2995</orcidid><orcidid>https://orcid.org/0000-0002-8304-2980</orcidid><orcidid>https://orcid.org/0000-0002-2913-2846</orcidid><orcidid>https://orcid.org/0000-0001-7178-1949</orcidid><orcidid>https://orcid.org/0000-0001-8631-5334</orcidid><orcidid>https://orcid.org/0000-0001-8517-9342</orcidid></search><sort><creationdate>20160906</creationdate><title>Influence of Adsorption on Proteins and Amyloid Detection by Silicon Nitride Nanopore</title><author>Balme, Sébastien ; Coulon, Pierre Eugène ; Lepoitevin, Mathilde ; Charlot, Benoît ; Yandrapalli, Naresh ; Favard, Cyril ; Muriaux, Delphine ; Bechelany, Mikhael ; Janot, Jean-Marc</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a448t-41e41430abfdcfcbea60168ed2a2ef08f150037d7eb06970ed3bb6c74cbbeb493</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Adsorption</topic><topic>Amyloid - analysis</topic><topic>Amyloid - chemistry</topic><topic>Avidin - analysis</topic><topic>Avidin - chemistry</topic><topic>Chemical Sciences</topic><topic>Electrochemical Techniques</topic><topic>Immunoglobulin G - analysis</topic><topic>Immunoglobulin G - chemistry</topic><topic>Interface Components: Nanops, Colloids, Emulsions, Surfactants, Proteins, Polymers</topic><topic>Kinetics</topic><topic>Muramidase - analysis</topic><topic>Muramidase - chemistry</topic><topic>Nanopores - ultrastructure</topic><topic>Silicon Compounds - chemistry</topic><topic>Solutions</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Balme, Sébastien</creatorcontrib><creatorcontrib>Coulon, Pierre Eugène</creatorcontrib><creatorcontrib>Lepoitevin, Mathilde</creatorcontrib><creatorcontrib>Charlot, Benoît</creatorcontrib><creatorcontrib>Yandrapalli, Naresh</creatorcontrib><creatorcontrib>Favard, Cyril</creatorcontrib><creatorcontrib>Muriaux, Delphine</creatorcontrib><creatorcontrib>Bechelany, Mikhael</creatorcontrib><creatorcontrib>Janot, Jean-Marc</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>Langmuir</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Balme, Sébastien</au><au>Coulon, Pierre Eugène</au><au>Lepoitevin, Mathilde</au><au>Charlot, Benoît</au><au>Yandrapalli, Naresh</au><au>Favard, Cyril</au><au>Muriaux, Delphine</au><au>Bechelany, Mikhael</au><au>Janot, Jean-Marc</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Influence of Adsorption on Proteins and Amyloid Detection by Silicon Nitride Nanopore</atitle><jtitle>Langmuir</jtitle><addtitle>Langmuir</addtitle><date>2016-09-06</date><risdate>2016</risdate><volume>32</volume><issue>35</issue><spage>8916</spage><epage>8925</epage><pages>8916-8925</pages><issn>0743-7463</issn><eissn>1520-5827</eissn><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 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.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>27506271</pmid><doi>10.1021/acs.langmuir.6b02048</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0003-0244-9939</orcidid><orcidid>https://orcid.org/0000-0003-0779-3384</orcidid><orcidid>https://orcid.org/0000-0002-0663-2995</orcidid><orcidid>https://orcid.org/0000-0002-8304-2980</orcidid><orcidid>https://orcid.org/0000-0002-2913-2846</orcidid><orcidid>https://orcid.org/0000-0001-7178-1949</orcidid><orcidid>https://orcid.org/0000-0001-8631-5334</orcidid><orcidid>https://orcid.org/0000-0001-8517-9342</orcidid></addata></record> |
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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 |
title | Influence of Adsorption on Proteins and Amyloid Detection by Silicon Nitride Nanopore |
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