Evaluation of backbone-cyclized HER2-binding 2-helix affibody molecule for in vivo molecular imaging.
Identifieur interne : 000716 ( Main/Exploration ); précédent : 000715; suivant : 000717Evaluation of backbone-cyclized HER2-binding 2-helix affibody molecule for in vivo molecular imaging.
Auteurs : RBID : pubmed:23357083English descriptors
- KwdEn :
- Animals, Cell Line, Tumor, Cyclization, Gallium Radioisotopes (diagnostic use), Heterocyclic Compounds, 1-Ring (chemistry), Humans, Indium Radioisotopes (diagnostic use), Mice, Molecular Imaging, Protein Stability, Protein Structure, Secondary, Receptor, erbB-2 (metabolism), Recombinant Fusion Proteins (chemistry), Recombinant Fusion Proteins (diagnostic use), Recombinant Fusion Proteins (metabolism), Substrate Specificity, Temperature.
- MESH :
- chemical , chemistry : Heterocyclic Compounds, 1-Ring, Recombinant Fusion Proteins.
- chemical , diagnostic use : Gallium Radioisotopes, Indium Radioisotopes, Recombinant Fusion Proteins.
- chemical , metabolism : Receptor, erbB-2, Recombinant Fusion Proteins.
- Animals, Cell Line, Tumor, Cyclization, Humans, Mice, Molecular Imaging, Protein Stability, Protein Structure, Secondary, Substrate Specificity, Temperature.
Abstract
Affibody molecules, small scaffold proteins, have demonstrated an appreciable potential as imaging probes. Affibody molecules are composed of three alpha-helices. Helices 1 and 2 are involved in molecular recognition, while helix 3 provides stability. The size of Affibody molecules can be reduced by omitting the third alpha-helix and cross-linking the two remaining, providing a smaller molecule with better extravasation and quicker clearance of unbound tracer. The goal of this study was to develop a novel 2-helix Affibody molecule based on backbone cyclization by native chemical ligation (NCL).
DOI: 10.1016/j.nucmedbio.2012.12.009
PubMed: 23357083
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Evaluation of backbone-cyclized HER2-binding 2-helix affibody molecule for in vivo molecular imaging.</title><author><name sortKey="Honarvar, Hadis" uniqKey="Honarvar H">Hadis Honarvar</name><affiliation wicri:level="1"><nlm:affiliation>Unit of Biomedical Radiation Sciences, Rudbeck Laboratory, Uppsala University, S-751 81 Uppsala, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Unit of Biomedical Radiation Sciences, Rudbeck Laboratory, Uppsala University, S-751 81 Uppsala</wicri:regionArea></affiliation></author><author><name sortKey="Jokilaakso, Nima" uniqKey="Jokilaakso N">Nima Jokilaakso</name></author><author><name sortKey="Andersson, Karl" uniqKey="Andersson K">Karl Andersson</name></author><author><name sortKey="Malmberg, Jennie" uniqKey="Malmberg J">Jennie Malmberg</name></author><author><name sortKey="Rosik, Daniel" uniqKey="Rosik D">Daniel Rosik</name></author><author><name sortKey="Orlova, Anna" uniqKey="Orlova A">Anna Orlova</name></author><author><name sortKey="Karlstr M, Amelie Eriksson" uniqKey="Karlstr M A">Amelie Eriksson Karlström</name></author><author><name sortKey="Tolmachev, Vladimir" uniqKey="Tolmachev V">Vladimir Tolmachev</name></author><author><name sortKey="J Rver, Peter" uniqKey="J Rver P">Peter Järver</name></author></titleStmt><publicationStmt><date when="2013">2013</date><idno type="doi">10.1016/j.nucmedbio.2012.12.009</idno><idno type="RBID">pubmed:23357083</idno><idno type="pmid">23357083</idno><idno type="wicri:Area/Main/Corpus">000830</idno><idno type="wicri:Area/Main/Curation">000830</idno><idno type="wicri:Area/Main/Exploration">000716</idno></publicationStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Cell Line, Tumor</term><term>Cyclization</term><term>Gallium Radioisotopes (diagnostic use)</term><term>Heterocyclic Compounds, 1-Ring (chemistry)</term><term>Humans</term><term>Indium Radioisotopes (diagnostic use)</term><term>Mice</term><term>Molecular Imaging</term><term>Protein Stability</term><term>Protein Structure, Secondary</term><term>Receptor, erbB-2 (metabolism)</term><term>Recombinant Fusion Proteins (chemistry)</term><term>Recombinant Fusion Proteins (diagnostic use)</term><term>Recombinant Fusion Proteins (metabolism)</term><term>Substrate Specificity</term><term>Temperature</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Heterocyclic Compounds, 1-Ring</term><term>Recombinant Fusion Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="diagnostic use" xml:lang="en"><term>Gallium Radioisotopes</term><term>Indium Radioisotopes</term><term>Recombinant Fusion Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Receptor, erbB-2</term><term>Recombinant Fusion Proteins</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Line, Tumor</term><term>Cyclization</term><term>Humans</term><term>Mice</term><term>Molecular Imaging</term><term>Protein Stability</term><term>Protein Structure, Secondary</term><term>Substrate Specificity</term><term>Temperature</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Affibody molecules, small scaffold proteins, have demonstrated an appreciable potential as imaging probes. Affibody molecules are composed of three alpha-helices. Helices 1 and 2 are involved in molecular recognition, while helix 3 provides stability. The size of Affibody molecules can be reduced by omitting the third alpha-helix and cross-linking the two remaining, providing a smaller molecule with better extravasation and quicker clearance of unbound tracer. The goal of this study was to develop a novel 2-helix Affibody molecule based on backbone cyclization by native chemical ligation (NCL).</div></front></TEI><pubmed><MedlineCitation Owner="NLM" Status="MEDLINE"><PMID Version="1">23357083</PMID><DateCreated><Year>2013</Year><Month>03</Month><Day>13</Day></DateCreated><DateCompleted><Year>2013</Year><Month>09</Month><Day>12</Day></DateCompleted><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1872-9614</ISSN><JournalIssue CitedMedium="Internet"><Volume>40</Volume><Issue>3</Issue><PubDate><Year>2013</Year><Month>Apr</Month></PubDate></JournalIssue><Title>Nuclear medicine and biology</Title><ISOAbbreviation>Nucl. Med. Biol.</ISOAbbreviation></Journal><ArticleTitle>Evaluation of backbone-cyclized HER2-binding 2-helix affibody molecule for in vivo molecular imaging.</ArticleTitle><Pagination><MedlinePgn>378-86</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.nucmedbio.2012.12.009</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0969-8051(12)00320-4</ELocationID><Abstract><AbstractText Label="INTRODUCTION" NlmCategory="BACKGROUND">Affibody molecules, small scaffold proteins, have demonstrated an appreciable potential as imaging probes. Affibody molecules are composed of three alpha-helices. Helices 1 and 2 are involved in molecular recognition, while helix 3 provides stability. The size of Affibody molecules can be reduced by omitting the third alpha-helix and cross-linking the two remaining, providing a smaller molecule with better extravasation and quicker clearance of unbound tracer. The goal of this study was to develop a novel 2-helix Affibody molecule based on backbone cyclization by native chemical ligation (NCL).</AbstractText><AbstractText Label="METHODS" NlmCategory="METHODS">The HER2-targeting NCL-cyclized Affibody molecule ZHER2:342min has been designed, synthesized and site-specifically conjugated with a DOTA chelator. DOTA-ZHER2:342min was labeled with (111)In and (68)Ga. The binding affinity of DOTA-ZHER2:342min was evaluated in vitro. The targeting properties of (111)In- and (68)Ga-DOTA-ZHER2:342min were evaluated in mice bearing SKOV-3 xenografts and compared with the properties of (111)In- and (68)Ga-labeled PEP09239, a DOTA-conjugated 2-helix Affibody analogue cyclized by a homocysteine disulfide bridge.</AbstractText><AbstractText Label="RESULTS" NlmCategory="RESULTS">The dissociation constant (KD) for DOTA-ZHER2:342min binding to HER2 was 18nM according to SPR measurements. DOTA-ZHER2:342min was labeled with (111)In and (68)Ga. Both conjugates demonstrated bi-phasic binding kinetics to HER2-expressing cells, with KD1 in low nanomolar range. Both variants demonstrated specific uptake in HER2-expressing xenografts. Tumor-to-blood ratios at 2h p.i. were 6.1±1.3 for (111)In- DOTA-ZHER2:342min and 4.6±0.7 for (68)Ga-DOTA-ZHER2:342min. However, the uptake of DOTA-ZHER2:342min in lung, liver and spleen was appreciably higher than the uptake of PEP09239-based counterparts.</AbstractText><AbstractText Label="CONCLUSIONS" NlmCategory="CONCLUSIONS">Native chemical ligation enables production of a backbone-cyclized HER2-binding 2-helix Affibody molecule (ZHER2:342min) with low nanomolar target affinity and specific tumor uptake.</AbstractText><CopyrightInformation>Copyright © 2013 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Honarvar</LastName><ForeName>Hadis</ForeName><Initials>H</Initials><Affiliation>Unit of Biomedical Radiation Sciences, Rudbeck Laboratory, Uppsala University, S-751 81 Uppsala, Sweden.</Affiliation></Author><Author ValidYN="Y"><LastName>Jokilaakso</LastName><ForeName>Nima</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Andersson</LastName><ForeName>Karl</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Malmberg</LastName><ForeName>Jennie</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Rosik</LastName><ForeName>Daniel</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Orlova</LastName><ForeName>Anna</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Karlström</LastName><ForeName>Amelie Eriksson</ForeName><Initials>AE</Initials></Author><Author ValidYN="Y"><LastName>Tolmachev</LastName><ForeName>Vladimir</ForeName><Initials>V</Initials></Author><Author ValidYN="Y"><LastName>Järver</LastName><ForeName>Peter</ForeName><Initials>P</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>2013</Year><Month>01</Month><Day>26</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Nucl Med Biol</MedlineTA><NlmUniqueID>9304420</NlmUniqueID><ISSNLinking>0969-8051</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance>Gallium Radioisotopes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance>Heterocyclic Compounds, 1-Ring</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance>Indium Radioisotopes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance>Recombinant Fusion Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance>affibody (ZHER2-342)2</NameOfSubstance></Chemical><Chemical><RegistryNumber>60239-18-1</RegistryNumber><NameOfSubstance>1,4,7,10-tetraazacyclododecane- 1,4,7,10-tetraacetic acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.10.1</RegistryNumber><NameOfSubstance>Receptor, erbB-2</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Cell Line, Tumor</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Cyclization</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Gallium Radioisotopes</DescriptorName><QualifierName MajorTopicYN="N">diagnostic use</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Heterocyclic Compounds, 1-Ring</DescriptorName><QualifierName MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Indium Radioisotopes</DescriptorName><QualifierName MajorTopicYN="N">diagnostic use</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Mice</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="Y">Molecular Imaging</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Protein Stability</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Protein Structure, Secondary</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Receptor, erbB-2</DescriptorName><QualifierName MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Recombinant Fusion Proteins</DescriptorName><QualifierName MajorTopicYN="N">chemistry</QualifierName><QualifierName MajorTopicYN="Y">diagnostic use</QualifierName><QualifierName MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Temperature</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2012</Year><Month>10</Month><Day>2</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2012</Year><Month>12</Month><Day>13</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2012</Year><Month>12</Month><Day>17</Day></PubMedPubDate><PubMedPubDate PubStatus="aheadofprint"><Year>2013</Year><Month>1</Month><Day>26</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2013</Year><Month>1</Month><Day>30</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2013</Year><Month>1</Month><Day>30</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2013</Year><Month>9</Month><Day>13</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pii">S0969-8051(12)00320-4</ArticleId><ArticleId IdType="doi">10.1016/j.nucmedbio.2012.12.009</ArticleId><ArticleId IdType="pubmed">23357083</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=IndiumV2/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000716 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000716 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= *** parameter Area/wikiCode missing ***
|area= IndiumV2
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:23357083
|texte= Evaluation of backbone-cyclized HER2-binding 2-helix affibody molecule for in vivo molecular imaging.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:23357083" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a IndiumV2
| This area was generated with Dilib version V0.5.76. |  |