Peptides for functionalization of InP semiconductors.
Identifieur interne : 001D21 ( Main/Exploration ); précédent : 001D20; suivant : 001D22Peptides for functionalization of InP semiconductors.
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Abstract
The challenge is to achieve high specificity in molecular sensing by proper functionalization of micro/nano-structured semiconductors by peptides that reveal specific recognition for these structures. Here we report on surface modification of the InP semiconductors by adhesion peptides produced by the phage display technique. An M13 bacteriophage library has been used to screen 10(10) different peptides against the InP(001) and the InP(111) surfaces to finally isolate specific peptides for each orientation of the InP. MALDI-TOF/TOF mass spectrometry has been employed to study real affinity of the peptide towards the InP surfaces. The peptides serve for controlled placement of biotin onto InP to bind then streptavidin. Our Atomic Force Microscopy study revealed a total surface coverage of molecules when the InP surface was functionalized by its specific biotinylated peptide (YAIKGPSHFRPS). Finally, fluorescence microscopy has been employed to demonstrate the preferential attachment of the peptide onto a micro-patterned InP surface. Use of substrate specific peptides could present an alternative solution for the problems encountered in the actually existing sensing methods and molecular self-assembly due to the unwanted unspecific interactions.
DOI: 10.1016/j.jcis.2009.05.040
PubMed: 19539948
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Peptides for functionalization of InP semiconductors.</title><author><name sortKey="Estephan, Elias" uniqKey="Estephan E">Elias Estephan</name><affiliation wicri:level="3"><nlm:affiliation>Groupe d'Etude des Semi-conducteurs, UMR 5650, CNRS-Université Montpellier II, 34095 Montpellier Cedex 5, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Groupe d'Etude des Semi-conducteurs, UMR 5650, CNRS-Université Montpellier II, 34095 Montpellier Cedex 5</wicri:regionArea><placeName><region type="region" nuts="2">Languedoc-Roussillon</region><settlement type="city">Montpellier</settlement></placeName></affiliation></author><author><name sortKey="Saab, Marie Belle" uniqKey="Saab M">Marie-belle Saab</name></author><author><name sortKey="Larroque, Christian" uniqKey="Larroque C">Christian Larroque</name></author><author><name sortKey="Martin, Marta" uniqKey="Martin M">Marta Martin</name></author><author><name sortKey="Olsson, Fredrik" uniqKey="Olsson F">Fredrik Olsson</name></author><author><name sortKey="Lourdudoss, Sebastian" uniqKey="Lourdudoss S">Sebastian Lourdudoss</name></author><author><name sortKey="Gergely, Csilla" uniqKey="Gergely C">Csilla Gergely</name></author></titleStmt><publicationStmt><date when="2009">2009</date><idno type="doi">10.1016/j.jcis.2009.05.040</idno><idno type="RBID">pubmed:19539948</idno><idno type="pmid">19539948</idno><idno type="wicri:Area/Main/Corpus">001E04</idno><idno type="wicri:Area/Main/Curation">001E04</idno><idno type="wicri:Area/Main/Exploration">001D21</idno></publicationStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Indium (chemistry)</term><term>Molecular Sequence Data</term><term>Peptides (chemistry)</term><term>Phosphines (chemistry)</term><term>Semiconductors</term><term>Spectrometry, Fluorescence</term><term>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Indium</term><term>Peptides</term><term>Phosphines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Molecular Sequence Data</term><term>Semiconductors</term><term>Spectrometry, Fluorescence</term><term>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The challenge is to achieve high specificity in molecular sensing by proper functionalization of micro/nano-structured semiconductors by peptides that reveal specific recognition for these structures. Here we report on surface modification of the InP semiconductors by adhesion peptides produced by the phage display technique. An M13 bacteriophage library has been used to screen 10(10) different peptides against the InP(001) and the InP(111) surfaces to finally isolate specific peptides for each orientation of the InP. MALDI-TOF/TOF mass spectrometry has been employed to study real affinity of the peptide towards the InP surfaces. The peptides serve for controlled placement of biotin onto InP to bind then streptavidin. Our Atomic Force Microscopy study revealed a total surface coverage of molecules when the InP surface was functionalized by its specific biotinylated peptide (YAIKGPSHFRPS). Finally, fluorescence microscopy has been employed to demonstrate the preferential attachment of the peptide onto a micro-patterned InP surface. Use of substrate specific peptides could present an alternative solution for the problems encountered in the actually existing sensing methods and molecular self-assembly due to the unwanted unspecific interactions.</div></front></TEI><pubmed><MedlineCitation Owner="NLM" Status="MEDLINE"><PMID Version="1">19539948</PMID><DateCreated><Year>2009</Year><Month>07</Month><Day>28</Day></DateCreated><DateCompleted><Year>2009</Year><Month>11</Month><Day>10</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1095-7103</ISSN><JournalIssue CitedMedium="Internet"><Volume>337</Volume><Issue>2</Issue><PubDate><Year>2009</Year><Month>Sep</Month><Day>15</Day></PubDate></JournalIssue><Title>Journal of colloid and interface science</Title><ISOAbbreviation>J Colloid Interface Sci</ISOAbbreviation></Journal><ArticleTitle>Peptides for functionalization of InP semiconductors.</ArticleTitle><Pagination><MedlinePgn>358-63</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.jcis.2009.05.040</ELocationID><Abstract><AbstractText>The challenge is to achieve high specificity in molecular sensing by proper functionalization of micro/nano-structured semiconductors by peptides that reveal specific recognition for these structures. Here we report on surface modification of the InP semiconductors by adhesion peptides produced by the phage display technique. An M13 bacteriophage library has been used to screen 10(10) different peptides against the InP(001) and the InP(111) surfaces to finally isolate specific peptides for each orientation of the InP. MALDI-TOF/TOF mass spectrometry has been employed to study real affinity of the peptide towards the InP surfaces. The peptides serve for controlled placement of biotin onto InP to bind then streptavidin. Our Atomic Force Microscopy study revealed a total surface coverage of molecules when the InP surface was functionalized by its specific biotinylated peptide (YAIKGPSHFRPS). Finally, fluorescence microscopy has been employed to demonstrate the preferential attachment of the peptide onto a micro-patterned InP surface. Use of substrate specific peptides could present an alternative solution for the problems encountered in the actually existing sensing methods and molecular self-assembly due to the unwanted unspecific interactions.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Estephan</LastName><ForeName>Elias</ForeName><Initials>E</Initials><Affiliation>Groupe d'Etude des Semi-conducteurs, UMR 5650, CNRS-Université Montpellier II, 34095 Montpellier Cedex 5, France.</Affiliation></Author><Author ValidYN="Y"><LastName>Saab</LastName><ForeName>Marie-belle</ForeName><Initials>MB</Initials></Author><Author ValidYN="Y"><LastName>Larroque</LastName><ForeName>Christian</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Martin</LastName><ForeName>Marta</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Olsson</LastName><ForeName>Fredrik</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Lourdudoss</LastName><ForeName>Sebastian</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Gergely</LastName><ForeName>Csilla</ForeName><Initials>C</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>2009</Year><Month>05</Month><Day>25</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Colloid Interface Sci</MedlineTA><NlmUniqueID>0043125</NlmUniqueID><ISSNLinking>0021-9797</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance>Peptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance>Phosphines</NameOfSubstance></Chemical><Chemical><RegistryNumber>045A6V3VFX</RegistryNumber><NameOfSubstance>Indium</NameOfSubstance></Chemical><Chemical><RegistryNumber>22398-80-7</RegistryNumber><NameOfSubstance>indium phosphide</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Indium</DescriptorName><QualifierName MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Peptides</DescriptorName><QualifierName MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Phosphines</DescriptorName><QualifierName MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="Y">Semiconductors</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Spectrometry, Fluorescence</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2009</Year><Month>4</Month><Day>10</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2009</Year><Month>5</Month><Day>18</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2009</Year><Month>5</Month><Day>18</Day></PubMedPubDate><PubMedPubDate PubStatus="aheadofprint"><Year>2009</Year><Month>5</Month><Day>25</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2009</Year><Month>6</Month><Day>23</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2009</Year><Month>6</Month><Day>23</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2009</Year><Month>11</Month><Day>11</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pii">S0021-9797(09)00708-5</ArticleId><ArticleId IdType="doi">10.1016/j.jcis.2009.05.040</ArticleId><ArticleId IdType="pubmed">19539948</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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