Synthetic peptides as receptors in affinity sensors: a feasibility study.
Identifieur interne : 003534 ( PubMed/Curation ); précédent : 003533; suivant : 003535Synthetic peptides as receptors in affinity sensors: a feasibility study.
Auteurs : D J Van Den Heuvel [Pays-Bas] ; R P Kooyman ; J W Drijfhout ; G W WellingSource :
- Analytical biochemistry [ 0003-2697 ] ; 1993.
Descripteurs français
- KwdFr :
- MESH :
- analyse : Protéines de l'enveloppe virale.
- immunologie : Peptides, Protéines de l'enveloppe virale.
- Anticorps monoclonaux, Or, Peptides, Sites de fixation, Techniques de biocapteur, Thiols, Études de faisabilité.
English descriptors
- KwdEn :
- MESH :
- chemical , analysis : Viral Envelope Proteins.
- chemical , chemistry : Gold, Peptides, Sulfhydryl Compounds.
- chemical , immunology : Peptides, Viral Envelope Proteins.
- chemical : Antibodies, Monoclonal.
- Binding Sites, Biosensing Techniques, Feasibility Studies.
Abstract
A relatively simple method for immobilizing synthetic peptides as a receptor onto a gold surface using the self-assembling monolayer (SAM) technique has been investigated. A synthetic peptide with an amino acid sequence similar to the 9-21 gD sequence of herpes simplex virus type 1 was modified with an alkylthiol chain and adsorbed in combination with an alkylthiol chain without peptide according to the SAM procedures. The resulting self-assembled receptor layers (SARs) were able to specifically interact with a monoclonal antibody directed against the 9-21 gD peptide. Binding studies monitored with a surface plasmon resonance setup showed that the response to the antibody depended on the composition of the SAR; a maximum response was reached at approximately 3 mol% peptide coverage. The response itself exceeded the value obtained from passive adsorption of the antibodies under similar conditions, indicating that the formed antibody layer is highly oriented. The equilibrium binding properties of the immobilized receptor molecules were found to be identical to those found when the immobilized antibodies interacted with the receptor molecule. The presence of a hydrophobic moiety in the alkylthiol derivates contributes to the ordering of the monolayer: a less specific interaction occurred when SARs without hydrophobic moiety were used.
DOI: 10.1006/abio.1993.1579
PubMed: 8122782
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: Pour aller vers cette notice dans l'étape Curation :003534
Links to Exploration step
pubmed:8122782Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Synthetic peptides as receptors in affinity sensors: a feasibility study.</title><author><name sortKey="Van Den Heuvel, D J" sort="Van Den Heuvel, D J" uniqKey="Van Den Heuvel D" first="D J" last="Van Den Heuvel">D J Van Den Heuvel</name><affiliation wicri:level="1"><nlm:affiliation>University of Twente, MESA-Institute, Department of Applied Physics, Enschede, The Netherlands.</nlm:affiliation><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>University of Twente, MESA-Institute, Department of Applied Physics, Enschede</wicri:regionArea></affiliation></author><author><name sortKey="Kooyman, R P" sort="Kooyman, R P" uniqKey="Kooyman R" first="R P" last="Kooyman">R P Kooyman</name></author><author><name sortKey="Drijfhout, J W" sort="Drijfhout, J W" uniqKey="Drijfhout J" first="J W" last="Drijfhout">J W Drijfhout</name></author><author><name sortKey="Welling, G W" sort="Welling, G W" uniqKey="Welling G" first="G W" last="Welling">G W Welling</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1993">1993</date><idno type="RBID">pubmed:8122782</idno><idno type="pmid">8122782</idno><idno type="doi">10.1006/abio.1993.1579</idno><idno type="wicri:Area/PubMed/Corpus">003534</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">003534</idno><idno type="wicri:Area/PubMed/Curation">003534</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">003534</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Synthetic peptides as receptors in affinity sensors: a feasibility study.</title><author><name sortKey="Van Den Heuvel, D J" sort="Van Den Heuvel, D J" uniqKey="Van Den Heuvel D" first="D J" last="Van Den Heuvel">D J Van Den Heuvel</name><affiliation wicri:level="1"><nlm:affiliation>University of Twente, MESA-Institute, Department of Applied Physics, Enschede, The Netherlands.</nlm:affiliation><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>University of Twente, MESA-Institute, Department of Applied Physics, Enschede</wicri:regionArea></affiliation></author><author><name sortKey="Kooyman, R P" sort="Kooyman, R P" uniqKey="Kooyman R" first="R P" last="Kooyman">R P Kooyman</name></author><author><name sortKey="Drijfhout, J W" sort="Drijfhout, J W" uniqKey="Drijfhout J" first="J W" last="Drijfhout">J W Drijfhout</name></author><author><name sortKey="Welling, G W" sort="Welling, G W" uniqKey="Welling G" first="G W" last="Welling">G W Welling</name></author></analytic><series><title level="j">Analytical biochemistry</title><idno type="ISSN">0003-2697</idno><imprint><date when="1993" type="published">1993</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Antibodies, Monoclonal</term><term>Binding Sites</term><term>Biosensing Techniques</term><term>Feasibility Studies</term><term>Gold (chemistry)</term><term>Peptides (chemistry)</term><term>Peptides (immunology)</term><term>Sulfhydryl Compounds (chemistry)</term><term>Viral Envelope Proteins (analysis)</term><term>Viral Envelope Proteins (immunology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Anticorps monoclonaux</term><term>Or ()</term><term>Peptides ()</term><term>Peptides (immunologie)</term><term>Protéines de l'enveloppe virale (analyse)</term><term>Protéines de l'enveloppe virale (immunologie)</term><term>Sites de fixation</term><term>Techniques de biocapteur</term><term>Thiols ()</term><term>Études de faisabilité</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Gold</term><term>Peptides</term><term>Sulfhydryl Compounds</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Peptides</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Antibodies, Monoclonal</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Protéines de l'enveloppe virale</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Peptides</term><term>Protéines de l'enveloppe virale</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term><term>Biosensing Techniques</term><term>Feasibility Studies</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Anticorps monoclonaux</term><term>Or</term><term>Peptides</term><term>Sites de fixation</term><term>Techniques de biocapteur</term><term>Thiols</term><term>Études de faisabilité</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A relatively simple method for immobilizing synthetic peptides as a receptor onto a gold surface using the self-assembling monolayer (SAM) technique has been investigated. A synthetic peptide with an amino acid sequence similar to the 9-21 gD sequence of herpes simplex virus type 1 was modified with an alkylthiol chain and adsorbed in combination with an alkylthiol chain without peptide according to the SAM procedures. The resulting self-assembled receptor layers (SARs) were able to specifically interact with a monoclonal antibody directed against the 9-21 gD peptide. Binding studies monitored with a surface plasmon resonance setup showed that the response to the antibody depended on the composition of the SAR; a maximum response was reached at approximately 3 mol% peptide coverage. The response itself exceeded the value obtained from passive adsorption of the antibodies under similar conditions, indicating that the formed antibody layer is highly oriented. The equilibrium binding properties of the immobilized receptor molecules were found to be identical to those found when the immobilized antibodies interacted with the receptor molecule. The presence of a hydrophobic moiety in the alkylthiol derivates contributes to the ordering of the monolayer: a less specific interaction occurred when SARs without hydrophobic moiety were used.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8122782</PMID><DateCompleted><Year>1994</Year><Month>04</Month><Day>06</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>28</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0003-2697</ISSN><JournalIssue CitedMedium="Print"><Volume>215</Volume><Issue>2</Issue><PubDate><Year>1993</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Analytical biochemistry</Title><ISOAbbreviation>Anal. Biochem.</ISOAbbreviation></Journal><ArticleTitle>Synthetic peptides as receptors in affinity sensors: a feasibility study.</ArticleTitle><Pagination><MedlinePgn>223-30</MedlinePgn></Pagination><Abstract><AbstractText>A relatively simple method for immobilizing synthetic peptides as a receptor onto a gold surface using the self-assembling monolayer (SAM) technique has been investigated. A synthetic peptide with an amino acid sequence similar to the 9-21 gD sequence of herpes simplex virus type 1 was modified with an alkylthiol chain and adsorbed in combination with an alkylthiol chain without peptide according to the SAM procedures. The resulting self-assembled receptor layers (SARs) were able to specifically interact with a monoclonal antibody directed against the 9-21 gD peptide. Binding studies monitored with a surface plasmon resonance setup showed that the response to the antibody depended on the composition of the SAR; a maximum response was reached at approximately 3 mol% peptide coverage. The response itself exceeded the value obtained from passive adsorption of the antibodies under similar conditions, indicating that the formed antibody layer is highly oriented. The equilibrium binding properties of the immobilized receptor molecules were found to be identical to those found when the immobilized antibodies interacted with the receptor molecule. The presence of a hydrophobic moiety in the alkylthiol derivates contributes to the ordering of the monolayer: a less specific interaction occurred when SARs without hydrophobic moiety were used.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>van den Heuvel</LastName><ForeName>D J</ForeName><Initials>DJ</Initials><AffiliationInfo><Affiliation>University of Twente, MESA-Institute, Department of Applied Physics, Enschede, The Netherlands.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kooyman</LastName><ForeName>R P</ForeName><Initials>RP</Initials></Author><Author ValidYN="Y"><LastName>Drijfhout</LastName><ForeName>J W</ForeName><Initials>JW</Initials></Author><Author ValidYN="Y"><LastName>Welling</LastName><ForeName>G W</ForeName><Initials>GW</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Anal Biochem</MedlineTA><NlmUniqueID>0370535</NlmUniqueID><ISSNLinking>0003-2697</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000911">Antibodies, Monoclonal</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010455">Peptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013438">Sulfhydryl Compounds</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014759">Viral Envelope Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C039447">glycoprotein D, Human herpesvirus 1</NameOfSubstance></Chemical><Chemical><RegistryNumber>7440-57-5</RegistryNumber><NameOfSubstance UI="D006046">Gold</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000911" MajorTopicYN="N">Antibodies, Monoclonal</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015374" MajorTopicYN="Y">Biosensing Techniques</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005240" MajorTopicYN="N">Feasibility Studies</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006046" MajorTopicYN="N">Gold</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010455" MajorTopicYN="N">Peptides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013438" MajorTopicYN="N">Sulfhydryl Compounds</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014759" MajorTopicYN="N">Viral Envelope Proteins</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1993</Year><Month>12</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1993</Year><Month>12</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1993</Year><Month>12</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">8122782</ArticleId><ArticleId IdType="pii">S0003269783715794</ArticleId><ArticleId IdType="doi">10.1006/abio.1993.1579</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/SrasV1/Data/PubMed/Curation
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 003534 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/PubMed/Curation/biblio.hfd -nk 003534 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= SrasV1
|flux= PubMed
|étape= Curation
|type= RBID
|clé= pubmed:8122782
|texte= Synthetic peptides as receptors in affinity sensors: a feasibility study.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Curation/RBID.i -Sk "pubmed:8122782" \
| HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Curation/biblio.hfd \
| NlmPubMed2Wicri -a SrasV1
| This area was generated with Dilib version V0.6.33. |  |