Localized surface plasmon resonance interfaces coated with poly[3-(pyrrolyl) carboxylic acid] for histidine-tagged peptide sensing
Identifieur interne : 002A66 ( Main/Repository ); précédent : 002A65; suivant : 002A67Localized surface plasmon resonance interfaces coated with poly[3-(pyrrolyl) carboxylic acid] for histidine-tagged peptide sensing
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- concept : Or.
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Abstract
The paper reports on a novel localized surface plasmon resonance (LSPR) substrate architecture for the immobilization and detection of histidine-tagged peptides. The LSPR interface consists of an ITO (indium tin oxide) substrate coated with gold nanostructures. The latter are obtained by thermal deposition of a thin (2 nm thick) gold film followed by post-annealing at 500 °C. The LSPR interface was coated with poly[3-(pyrrolyl)carboxylic acid] thin films using electrochemical means. The ability of the LSPR interfaces coated with poly[3-(pyrrolyl)carboxylic acid] to chelate copper ions was investigated. Once loaded with metal ions, the modified LSPR interface was able to bind specifically to histidine-tagged peptides. The binding process was followed using LSPR.
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<author><name sortKey="Tighilt, Fatma Zohra" uniqKey="Tighilt F">Fatma-Zohra Tighilt</name>
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<author><name sortKey="Szunerits, Sabine" uniqKey="Szunerits S">Sabine Szunerits</name>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Annealing</term>
<term>Carboxylic acid</term>
<term>Copper ion</term>
<term>Deposition</term>
<term>Detection</term>
<term>Electrochemical method</term>
<term>Gold</term>
<term>Histidine</term>
<term>Immobilization</term>
<term>Indium oxide</term>
<term>Interface</term>
<term>Metal ion</term>
<term>Nanostructure</term>
<term>Peptides</term>
<term>Substrate</term>
<term>Surface plasmon resonance</term>
<term>Thick film</term>
<term>Thin film</term>
<term>Tin oxide</term>
</keywords>
<keywords scheme="Pascal" xml:lang="fr"><term>Résonance plasmon surface</term>
<term>Interface</term>
<term>Substrat</term>
<term>Immobilisation</term>
<term>Détection</term>
<term>Or</term>
<term>Nanostructure</term>
<term>Dépôt</term>
<term>Couche épaisse</term>
<term>Recuit</term>
<term>Couche mince</term>
<term>Méthode électrochimique</term>
<term>Ion métallique</term>
<term>Acide carboxylique</term>
<term>Histidine</term>
<term>Peptide</term>
<term>Oxyde d'indium</term>
<term>Oxyde d'étain</term>
<term>Ion cuivre</term>
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<front><div type="abstract" xml:lang="en">The paper reports on a novel localized surface plasmon resonance (LSPR) substrate architecture for the immobilization and detection of histidine-tagged peptides. The LSPR interface consists of an ITO (indium tin oxide) substrate coated with gold nanostructures. The latter are obtained by thermal deposition of a thin (2 nm thick) gold film followed by post-annealing at 500 °C. The LSPR interface was coated with poly[3-(pyrrolyl)carboxylic acid] thin films using electrochemical means. The ability of the LSPR interfaces coated with poly[3-(pyrrolyl)carboxylic acid] to chelate copper ions was investigated. Once loaded with metal ions, the modified LSPR interface was able to bind specifically to histidine-tagged peptides. The binding process was followed using LSPR.</div>
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<fC01 i1="01" l="ENG"><s0>The paper reports on a novel localized surface plasmon resonance (LSPR) substrate architecture for the immobilization and detection of histidine-tagged peptides. The LSPR interface consists of an ITO (indium tin oxide) substrate coated with gold nanostructures. The latter are obtained by thermal deposition of a thin (2 nm thick) gold film followed by post-annealing at 500 °C. The LSPR interface was coated with poly[3-(pyrrolyl)carboxylic acid] thin films using electrochemical means. The ability of the LSPR interfaces coated with poly[3-(pyrrolyl)carboxylic acid] to chelate copper ions was investigated. Once loaded with metal ions, the modified LSPR interface was able to bind specifically to histidine-tagged peptides. The binding process was followed using LSPR.</s0>
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<s5>02</s5>
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<s5>02</s5>
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<s5>02</s5>
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<s5>03</s5>
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<s5>04</s5>
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<s5>04</s5>
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<s5>05</s5>
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<s5>05</s5>
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<s2>NC</s2>
<s5>06</s5>
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<s2>NC</s2>
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<s5>08</s5>
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<s5>12</s5>
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<s5>13</s5>
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<s5>13</s5>
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<s5>16</s5>
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