Predicting and rationalizing the effect of surface charge distribution and orientation on nano-wire based FET bio-sensors.
Identifieur interne : 001198 ( Main/Exploration ); précédent : 001197; suivant : 001199Predicting and rationalizing the effect of surface charge distribution and orientation on nano-wire based FET bio-sensors.
Auteurs : RBID : pubmed:21811738English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Capsid Proteins, Indium, Streptavidin.
- chemical , metabolism : Capsid Proteins, Streptavidin.
- chemistry : Nanowires.
- Biosensing Techniques, Protein Binding, Static Electricity, Transistors, Electronic.
Abstract
A single charge screening model of surface charge sensors in liquids (De Vico et al., Nanoscale, 2011, 3, 706-717) is extended to multiple charges to model the effect of the charge distributions of analyte proteins on FET sensor response. With this model we show that counter-intuitive signal changes (e.g. a positive signal change due to a net positive protein binding to a p-type conductor) can occur for certain combinations of charge distributions and Debye lengths. The new method is applied to interpret published experimental data on Streptavidin (Ishikawa et al., ACS Nano, 2009, 3, 3969-3976) and Nucleocapsid protein (Ishikawa et al., ACS Nano, 2009, 3, 1219-1224).
DOI: 10.1039/c1nr10316d
PubMed: 21811738
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Predicting and rationalizing the effect of surface charge distribution and orientation on nano-wire based FET bio-sensors.</title><author><name sortKey="De Vico, Luca" uniqKey="De Vico L">Luca De Vico</name><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry, University of Copenhagen, Universitetsparken 5, DK-2100, Copenhagen, Denmark. luca@chem.ku.dk</nlm:affiliation><country xml:lang="fr">Danemark</country><wicri:regionArea>Department of Chemistry, University of Copenhagen, Universitetsparken 5, DK-2100, Copenhagen</wicri:regionArea></affiliation></author><author><name sortKey="Iversen, Lars" uniqKey="Iversen L">Lars Iversen</name></author><author><name sortKey="S Rensen, Martin H" uniqKey="S Rensen M">Martin H Sørensen</name></author><author><name sortKey="Brandbyge, Mads" uniqKey="Brandbyge M">Mads Brandbyge</name></author><author><name sortKey="Nyg Rd, Jesper" uniqKey="Nyg Rd J">Jesper Nygård</name></author><author><name sortKey="Martinez, Karen L" uniqKey="Martinez K">Karen L Martinez</name></author><author><name sortKey="Jensen, Jan H" uniqKey="Jensen J">Jan H Jensen</name></author></titleStmt><publicationStmt><date when="2011">2011</date><idno type="doi">10.1039/c1nr10316d</idno><idno type="RBID">pubmed:21811738</idno><idno type="pmid">21811738</idno><idno type="wicri:Area/Main/Corpus">001233</idno><idno type="wicri:Area/Main/Curation">001233</idno><idno type="wicri:Area/Main/Exploration">001198</idno></publicationStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Biosensing Techniques</term><term>Capsid Proteins (chemistry)</term><term>Capsid Proteins (metabolism)</term><term>Indium (chemistry)</term><term>Nanowires (chemistry)</term><term>Protein Binding</term><term>Static Electricity</term><term>Streptavidin (chemistry)</term><term>Streptavidin (metabolism)</term><term>Transistors, Electronic</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Capsid Proteins</term><term>Indium</term><term>Streptavidin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Capsid Proteins</term><term>Streptavidin</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Nanowires</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Biosensing Techniques</term><term>Protein Binding</term><term>Static Electricity</term><term>Transistors, Electronic</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A single charge screening model of surface charge sensors in liquids (De Vico et al., Nanoscale, 2011, 3, 706-717) is extended to multiple charges to model the effect of the charge distributions of analyte proteins on FET sensor response. With this model we show that counter-intuitive signal changes (e.g. a positive signal change due to a net positive protein binding to a p-type conductor) can occur for certain combinations of charge distributions and Debye lengths. The new method is applied to interpret published experimental data on Streptavidin (Ishikawa et al., ACS Nano, 2009, 3, 3969-3976) and Nucleocapsid protein (Ishikawa et al., ACS Nano, 2009, 3, 1219-1224).</div></front></TEI><pubmed><MedlineCitation Owner="NLM" Status="MEDLINE"><PMID Version="1">21811738</PMID><DateCreated><Year>2011</Year><Month>09</Month><Day>02</Day></DateCreated><DateCompleted><Year>2012</Year><Month>01</Month><Day>03</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">2040-3372</ISSN><JournalIssue CitedMedium="Internet"><Volume>3</Volume><Issue>9</Issue><PubDate><Year>2011</Year><Month>Sep</Month><Day>1</Day></PubDate></JournalIssue><Title>Nanoscale</Title><ISOAbbreviation>Nanoscale</ISOAbbreviation></Journal><ArticleTitle>Predicting and rationalizing the effect of surface charge distribution and orientation on nano-wire based FET bio-sensors.</ArticleTitle><Pagination><MedlinePgn>3635-40</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1039/c1nr10316d</ELocationID><Abstract><AbstractText>A single charge screening model of surface charge sensors in liquids (De Vico et al., Nanoscale, 2011, 3, 706-717) is extended to multiple charges to model the effect of the charge distributions of analyte proteins on FET sensor response. With this model we show that counter-intuitive signal changes (e.g. a positive signal change due to a net positive protein binding to a p-type conductor) can occur for certain combinations of charge distributions and Debye lengths. The new method is applied to interpret published experimental data on Streptavidin (Ishikawa et al., ACS Nano, 2009, 3, 3969-3976) and Nucleocapsid protein (Ishikawa et al., ACS Nano, 2009, 3, 1219-1224).</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>De Vico</LastName><ForeName>Luca</ForeName><Initials>L</Initials><Affiliation>Department of Chemistry, University of Copenhagen, Universitetsparken 5, DK-2100, Copenhagen, Denmark. luca@chem.ku.dk</Affiliation></Author><Author ValidYN="Y"><LastName>Iversen</LastName><ForeName>Lars</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Sørensen</LastName><ForeName>Martin H</ForeName><Initials>MH</Initials></Author><Author ValidYN="Y"><LastName>Brandbyge</LastName><ForeName>Mads</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Nygård</LastName><ForeName>Jesper</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Martinez</LastName><ForeName>Karen L</ForeName><Initials>KL</Initials></Author><Author ValidYN="Y"><LastName>Jensen</LastName><ForeName>Jan H</ForeName><Initials>JH</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType>Journal Article</PublicationType><PublicationType>Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2011</Year><Month>08</Month><Day>03</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Nanoscale</MedlineTA><NlmUniqueID>101525249</NlmUniqueID><ISSNLinking>2040-3364</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance>Capsid Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>045A6V3VFX</RegistryNumber><NameOfSubstance>Indium</NameOfSubstance></Chemical><Chemical><RegistryNumber>4OO9KME22D</RegistryNumber><NameOfSubstance>indium oxide</NameOfSubstance></Chemical><Chemical><RegistryNumber>9013-20-1</RegistryNumber><NameOfSubstance>Streptavidin</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName MajorTopicYN="N">Biosensing Techniques</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Capsid Proteins</DescriptorName><QualifierName MajorTopicYN="N">chemistry</QualifierName><QualifierName MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Indium</DescriptorName><QualifierName MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Nanowires</DescriptorName><QualifierName MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Static Electricity</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Streptavidin</DescriptorName><QualifierName MajorTopicYN="N">chemistry</QualifierName><QualifierName MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Transistors, Electronic</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="aheadofprint"><Year>2011</Year><Month>8</Month><Day>3</Day></PubMedPubDate><PubMedPubDate PubStatus="epublish"><Year>2011</Year><Month>9</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2011</Year><Month>8</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2011</Year><Month>8</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2012</Year><Month>1</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="doi">10.1039/c1nr10316d</ArticleId><ArticleId IdType="pubmed">21811738</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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