Tumor targeting using affibody molecules: interplay of affinity, target expression level, and binding site composition.
Identifieur interne : 000961 ( Main/Exploration ); précédent : 000960; suivant : 000962Tumor targeting using affibody molecules: interplay of affinity, target expression level, and binding site composition.
Auteurs : RBID : pubmed:22586147English descriptors
- KwdEn :
- MESH :
- chemical , diagnostic use : Indium Radioisotopes.
- chemical , metabolism : Receptor, erbB-2.
- radionuclide imaging : Neoplasms, Experimental.
- Amino Acid Sequence, Animals, Binding Sites, Female, Isotope Labeling, Mice, Mice, Inbred BALB C, Molecular Sequence Data.
Abstract
Radionuclide imaging of cancer-associated molecular alterations may contribute to patient stratification for targeting therapy. Scaffold high-affinity proteins, such as Affibody molecules, are a new, promising class of probes for in vivo imaging.
DOI: 10.2967/jnumed.111.101527
PubMed: 22586147
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Tumor targeting using affibody molecules: interplay of affinity, target expression level, and binding site composition.</title><author><name sortKey="Tolmachev, Vladimir" uniqKey="Tolmachev V">Vladimir Tolmachev</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biomedical Radiation Sciences, Uppsala University, Uppsala, Sweden. vladimir.tolmachev@bms.uu.se</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Biomedical Radiation Sciences, Uppsala University, Uppsala</wicri:regionArea></affiliation></author><author><name sortKey="Tran, Thuy A" uniqKey="Tran T">Thuy A Tran</name></author><author><name sortKey="Rosik, Daniel" uniqKey="Rosik D">Daniel Rosik</name></author><author><name sortKey="Sj Berg, Anna" uniqKey="Sj Berg A">Anna Sjöberg</name></author><author><name sortKey="Abrahmsen, Lars" uniqKey="Abrahmsen L">Lars Abrahmsén</name></author><author><name sortKey="Orlova, Anna" uniqKey="Orlova A">Anna Orlova</name></author></titleStmt><publicationStmt><date when="2012">2012</date><idno type="doi">10.2967/jnumed.111.101527</idno><idno type="RBID">pubmed:22586147</idno><idno type="pmid">22586147</idno><idno type="wicri:Area/Main/Corpus">000D11</idno><idno type="wicri:Area/Main/Curation">000D11</idno><idno type="wicri:Area/Main/Exploration">000961</idno></publicationStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Binding Sites</term><term>Female</term><term>Indium Radioisotopes (diagnostic use)</term><term>Isotope Labeling</term><term>Mice</term><term>Mice, Inbred BALB C</term><term>Molecular Sequence Data</term><term>Neoplasms, Experimental (radionuclide imaging)</term><term>Receptor, erbB-2 (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="diagnostic use" xml:lang="en"><term>Indium Radioisotopes</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Receptor, erbB-2</term></keywords><keywords scheme="MESH" qualifier="radionuclide imaging" xml:lang="en"><term>Neoplasms, Experimental</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Binding Sites</term><term>Female</term><term>Isotope Labeling</term><term>Mice</term><term>Mice, Inbred BALB C</term><term>Molecular Sequence Data</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Radionuclide imaging of cancer-associated molecular alterations may contribute to patient stratification for targeting therapy. Scaffold high-affinity proteins, such as Affibody molecules, are a new, promising class of probes for in vivo imaging.</div></front></TEI><pubmed><MedlineCitation Owner="NLM" Status="MEDLINE"><PMID Version="1">22586147</PMID><DateCreated><Year>2012</Year><Month>06</Month><Day>04</Day></DateCreated><DateCompleted><Year>2012</Year><Month>08</Month><Day>07</Day></DateCompleted><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1535-5667</ISSN><JournalIssue CitedMedium="Internet"><Volume>53</Volume><Issue>6</Issue><PubDate><Year>2012</Year><Month>Jun</Month></PubDate></JournalIssue><Title>Journal of nuclear medicine : official publication, Society of Nuclear Medicine</Title><ISOAbbreviation>J. Nucl. Med.</ISOAbbreviation></Journal><ArticleTitle>Tumor targeting using affibody molecules: interplay of affinity, target expression level, and binding site composition.</ArticleTitle><Pagination><MedlinePgn>953-60</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.2967/jnumed.111.101527</ELocationID><Abstract><AbstractText Label="UNLABELLED">Radionuclide imaging of cancer-associated molecular alterations may contribute to patient stratification for targeting therapy. Scaffold high-affinity proteins, such as Affibody molecules, are a new, promising class of probes for in vivo imaging.</AbstractText><AbstractText Label="METHODS" NlmCategory="METHODS">The effects of human epidermal growth factor receptor 2 (HER2) affinity and binding site composition of HER2-binding Affibody molecules, and of the HER2 density on the tumor targeting, were studied in vivo. The tumor uptake and tumor-to-organ ratios of Affibody molecules with moderate (dissociation constant [K(D)] = 10(-9) M) or high (K(D) = 10(-10) M) affinity were compared between tumor xenografts with a high (SKOV-3) and low (LS174T) HER2 expression level in BALB/C nu/nu mice. Two Affibody molecules with similar affinity (K(D) = 10(-10) M) but having alternative amino acids in the binding site were compared.</AbstractText><AbstractText Label="RESULTS" NlmCategory="RESULTS">In SKOV-3 xenografts, uptake was independent of affinity at 4 h after injection, but high-affinity binders provided 2-fold-higher tumor radioactivity retention at 24 h. In LS174T xenografts, uptake of high-affinity probes was already severalfold higher at 4 h after injection, and the difference was increased at 24 h. The clearance rate and tumor-to-organ ratios were influenced by the amino acid composition of the binding surface of the tracer protein.</AbstractText><AbstractText Label="CONCLUSION" NlmCategory="CONCLUSIONS">The optimal affinity of HER2-binding Affibody molecules depends on the expression of a molecular target. At a high expression level (>10(6) receptors per cell), an affinity in the low-nanomolar range is sufficient. At moderate expression, subnanomolar affinity is desirable. The binding site composition can influence the imaging contrast. This information may be useful for development of imaging agents based on scaffold affinity proteins.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Tolmachev</LastName><ForeName>Vladimir</ForeName><Initials>V</Initials><Affiliation>Department of Biomedical Radiation Sciences, Uppsala University, Uppsala, Sweden. vladimir.tolmachev@bms.uu.se</Affiliation></Author><Author ValidYN="Y"><LastName>Tran</LastName><ForeName>Thuy A</ForeName><Initials>TA</Initials></Author><Author ValidYN="Y"><LastName>Rosik</LastName><ForeName>Daniel</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Sjöberg</LastName><ForeName>Anna</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Abrahmsén</LastName><ForeName>Lars</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Orlova</LastName><ForeName>Anna</ForeName><Initials>A</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>2012</Year><Month>05</Month><Day>14</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Nucl Med</MedlineTA><NlmUniqueID>0217410</NlmUniqueID><ISSNLinking>0161-5505</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance>Indium Radioisotopes</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">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Female</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Indium Radioisotopes</DescriptorName><QualifierName MajorTopicYN="Y">diagnostic use</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Isotope Labeling</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Mice</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Mice, Inbred BALB C</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Neoplasms, Experimental</DescriptorName><QualifierName MajorTopicYN="Y">radionuclide imaging</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Receptor, erbB-2</DescriptorName><QualifierName MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="aheadofprint"><Year>2012</Year><Month>5</Month><Day>14</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2012</Year><Month>5</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2012</Year><Month>5</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2012</Year><Month>8</Month><Day>8</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pii">jnumed.111.101527</ArticleId><ArticleId IdType="doi">10.2967/jnumed.111.101527</ArticleId><ArticleId IdType="pubmed">22586147</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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