Heterotetramers formed by an S-layer-streptavidin fusion protein and core-streptavidin as a nanoarrayed template for biochip development.
Identifieur interne : 002D21 ( Main/Exploration ); précédent : 002D20; suivant : 002D22Heterotetramers formed by an S-layer-streptavidin fusion protein and core-streptavidin as a nanoarrayed template for biochip development.
Auteurs : Carina Huber [Autriche] ; Jing Liu ; Eva M. Egelseer ; Dieter Moll ; Wolfgang Knoll ; Uwe B. Sleytr ; Margit SáraSource :
- Small (Weinheim an der Bergstrasse, Germany) [ 1613-6829 ] ; 2006.
Descripteurs français
- KwdFr :
- Biotinylation, Complexes multiprotéiques (), Conformation moléculaire, Cristallisation (), Dimérisation, Nanostructures (), Nanostructures (ultrastructure), Nanotechnologie (), Nanotechnologie (instrumentation), Propriétés de surface, Protéines de fusion recombinantes (), Résonance plasmonique de surface (), Streptavidine (), Séquençage par oligonucléotides en batterie (), Séquençage par oligonucléotides en batterie (instrumentation), Taille de particule, Technique FISH (), Test de matériaux.
- MESH :
- Biotinylation, Complexes multiprotéiques, Conformation moléculaire, Cristallisation, Dimérisation, Nanostructures, Nanotechnologie, Propriétés de surface, Protéines de fusion recombinantes, Résonance plasmonique de surface, Streptavidine, Séquençage par oligonucléotides en batterie, Taille de particule, Technique FISH, Test de matériaux.
English descriptors
- KwdEn :
- Biotinylation, Crystallization (methods), Dimerization, In Situ Hybridization, Fluorescence (methods), Materials Testing, Molecular Conformation, Multiprotein Complexes (chemistry), Nanostructures (chemistry), Nanostructures (ultrastructure), Nanotechnology (instrumentation), Nanotechnology (methods), Oligonucleotide Array Sequence Analysis (instrumentation), Oligonucleotide Array Sequence Analysis (methods), Particle Size, Recombinant Fusion Proteins (chemistry), Streptavidin (chemistry), Surface Plasmon Resonance (methods), Surface Properties.
- MESH :
- chemical , chemistry : Multiprotein Complexes, Recombinant Fusion Proteins, Streptavidin.
- chemistry : Nanostructures.
- instrumentation : Nanotechnology, Oligonucleotide Array Sequence Analysis.
- methods : Crystallization, In Situ Hybridization, Fluorescence, Nanotechnology, Oligonucleotide Array Sequence Analysis, Surface Plasmon Resonance.
- ultrastructure : Nanostructures.
- Biotinylation, Dimerization, Materials Testing, Molecular Conformation, Particle Size, Surface Properties.
Abstract
Based on the S-layer protein SbpA of Bacillus sphaericus CCM 2177, an S-layer-streptavidin fusion protein was constructed. After heterologous expression, isolation of the fusion protein, and refolding, functional heterotetramers were obtained that had retained the ability to recrystallize into the square-lattice structure on plain gold chips and on gold chips precoated with secondary cell wall polymer (SCWP), which is the natural anchoring molecule for the S-layer protein in the bacterial cell wall. Monolayers generated by recrystallization of heterotetramers on plain gold chips or on gold chips precoated with thiolated SCWP were exploited for the binding of biotinylated oligonucleotides (30-mers). Hybridization experiments with complementary fluorescently labeled oligonucleotides carrying one mismatch or no mismatch (both 15-mers) were performed and evaluated with surface-plasmon-field-enhanced fluorescence spectroscopy. For surfaces generated by the recrystallization of heterotetramers on SCWP-coated gold chips, a detection limit of 1.57 pM could be determined, whereas for surfaces obtained by direct recrystallization of heterotetramers on plain gold chips, a detection limit of 8.2 pM was found. Measuring the association and dissociation processes of oligonucleotides carrying no mismatch led to a dissociation constant of K(D)=6.3 x 10(-10) m, whereas for oligonucleotides carrying one mismatch a dissociation constant of K(D)=7.9 x 10(-9) m was determined. This finding was confirmed by measuring the whole Langmuir isotherm, which resulted in a dissociation constant of K(D)=2.6 x 10(-8) m.
DOI: 10.1002/smll.200500147
PubMed: 17193570
Affiliations:
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Le document en format XML
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Egelseer</name></author><author><name sortKey="Moll, Dieter" sort="Moll, Dieter" uniqKey="Moll D" first="Dieter" last="Moll">Dieter Moll</name></author><author><name sortKey="Knoll, Wolfgang" sort="Knoll, Wolfgang" uniqKey="Knoll W" first="Wolfgang" last="Knoll">Wolfgang Knoll</name></author><author><name sortKey="Sleytr, Uwe B" sort="Sleytr, Uwe B" uniqKey="Sleytr U" first="Uwe B" last="Sleytr">Uwe B. Sleytr</name></author><author><name sortKey="Sara, Margit" sort="Sara, Margit" uniqKey="Sara M" first="Margit" last="Sára">Margit Sára</name></author></analytic><series><title level="j">Small (Weinheim an der Bergstrasse, Germany)</title><idno type="eISSN">1613-6829</idno><imprint><date when="2006" type="published">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Biotinylation</term><term>Crystallization (methods)</term><term>Dimerization</term><term>In Situ Hybridization, Fluorescence (methods)</term><term>Materials Testing</term><term>Molecular Conformation</term><term>Multiprotein Complexes (chemistry)</term><term>Nanostructures (chemistry)</term><term>Nanostructures (ultrastructure)</term><term>Nanotechnology (instrumentation)</term><term>Nanotechnology (methods)</term><term>Oligonucleotide Array Sequence Analysis (instrumentation)</term><term>Oligonucleotide Array Sequence Analysis (methods)</term><term>Particle Size</term><term>Recombinant Fusion Proteins (chemistry)</term><term>Streptavidin (chemistry)</term><term>Surface Plasmon Resonance (methods)</term><term>Surface Properties</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Biotinylation</term><term>Complexes multiprotéiques ()</term><term>Conformation moléculaire</term><term>Cristallisation ()</term><term>Dimérisation</term><term>Nanostructures ()</term><term>Nanostructures (ultrastructure)</term><term>Nanotechnologie ()</term><term>Nanotechnologie (instrumentation)</term><term>Propriétés de surface</term><term>Protéines de fusion recombinantes ()</term><term>Résonance plasmonique de surface ()</term><term>Streptavidine ()</term><term>Séquençage par oligonucléotides en batterie ()</term><term>Séquençage par oligonucléotides en batterie (instrumentation)</term><term>Taille de particule</term><term>Technique FISH ()</term><term>Test de matériaux</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Multiprotein Complexes</term><term>Recombinant Fusion Proteins</term><term>Streptavidin</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Nanostructures</term></keywords><keywords scheme="MESH" qualifier="instrumentation" xml:lang="en"><term>Nanotechnology</term><term>Oligonucleotide Array Sequence Analysis</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Crystallization</term><term>In Situ Hybridization, Fluorescence</term><term>Nanotechnology</term><term>Oligonucleotide Array Sequence Analysis</term><term>Surface Plasmon Resonance</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="en"><term>Nanostructures</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Biotinylation</term><term>Dimerization</term><term>Materials Testing</term><term>Molecular Conformation</term><term>Particle Size</term><term>Surface Properties</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Biotinylation</term><term>Complexes multiprotéiques</term><term>Conformation moléculaire</term><term>Cristallisation</term><term>Dimérisation</term><term>Nanostructures</term><term>Nanotechnologie</term><term>Propriétés de surface</term><term>Protéines de fusion recombinantes</term><term>Résonance plasmonique de surface</term><term>Streptavidine</term><term>Séquençage par oligonucléotides en batterie</term><term>Taille de particule</term><term>Technique FISH</term><term>Test de matériaux</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Based on the S-layer protein SbpA of Bacillus sphaericus CCM 2177, an S-layer-streptavidin fusion protein was constructed. After heterologous expression, isolation of the fusion protein, and refolding, functional heterotetramers were obtained that had retained the ability to recrystallize into the square-lattice structure on plain gold chips and on gold chips precoated with secondary cell wall polymer (SCWP), which is the natural anchoring molecule for the S-layer protein in the bacterial cell wall. Monolayers generated by recrystallization of heterotetramers on plain gold chips or on gold chips precoated with thiolated SCWP were exploited for the binding of biotinylated oligonucleotides (30-mers). Hybridization experiments with complementary fluorescently labeled oligonucleotides carrying one mismatch or no mismatch (both 15-mers) were performed and evaluated with surface-plasmon-field-enhanced fluorescence spectroscopy. For surfaces generated by the recrystallization of heterotetramers on SCWP-coated gold chips, a detection limit of 1.57 pM could be determined, whereas for surfaces obtained by direct recrystallization of heterotetramers on plain gold chips, a detection limit of 8.2 pM was found. Measuring the association and dissociation processes of oligonucleotides carrying no mismatch led to a dissociation constant of K(D)=6.3 x 10(-10) m, whereas for oligonucleotides carrying one mismatch a dissociation constant of K(D)=7.9 x 10(-9) m was determined. This finding was confirmed by measuring the whole Langmuir isotherm, which resulted in a dissociation constant of K(D)=2.6 x 10(-8) m.</div></front></TEI><affiliations><list><country><li>Autriche</li></country><region><li>Vienne (Autriche)</li></region><settlement><li>Vienne (Autriche)</li></settlement></list><tree><noCountry><name sortKey="Egelseer, Eva M" sort="Egelseer, Eva M" uniqKey="Egelseer E" first="Eva M" last="Egelseer">Eva M. Egelseer</name><name sortKey="Knoll, Wolfgang" sort="Knoll, Wolfgang" uniqKey="Knoll W" first="Wolfgang" last="Knoll">Wolfgang Knoll</name><name sortKey="Liu, Jing" sort="Liu, Jing" uniqKey="Liu J" first="Jing" last="Liu">Jing Liu</name><name sortKey="Moll, Dieter" sort="Moll, Dieter" uniqKey="Moll D" first="Dieter" last="Moll">Dieter Moll</name><name sortKey="Sara, Margit" sort="Sara, Margit" uniqKey="Sara M" first="Margit" last="Sára">Margit Sára</name><name sortKey="Sleytr, Uwe B" sort="Sleytr, Uwe B" uniqKey="Sleytr U" first="Uwe B" last="Sleytr">Uwe B. Sleytr</name></noCountry><country name="Autriche"><region name="Vienne (Autriche)"><name sortKey="Huber, Carina" sort="Huber, Carina" uniqKey="Huber C" first="Carina" last="Huber">Carina Huber</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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