Affibody molecules for in vivo characterization of HER2-positive tumors by near-infrared imaging
Clinical Cancer Research, ISSN: 1078-0432, Vol: 14, Issue: 12, Page: 3840-3849
2008
- 150Citations
- 102Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations150
- Citation Indexes150
- 150
- CrossRef129
- Captures102
- Readers102
- 102
Article Description
Purpose: HER2 overexpression has been associated with a poor prognosis and resistance to therapy in breast cancer patients. We are developing molecular probes for in vivo quantitative imaging of HER2 receptors using near-infrared (NIR) optical imaging. The goal is to provide probes that will minimally interfere with the studied system, that is, whose binding does not interfere with the binding of the therapeutic agents and whose effect on the target cells is minimal. Experimental Design: We used three different types of HER2-specific Affibody molecules [monomer Z, dimer (Z, and albumin-binding domain-fused-(Z] as targeting agents and labeled them with Alexa Fluor dyes.Trastuzumab was also conjugated, using commercially available kits, as a standard control. The resulting conjugates were characterized in vitro by toxicity assays, Biacore affinity measurements, flow cytometry, and confocal microscopy. Semiquantitative in vivo NIR optical imaging studies were carried out using mice with s.c. xenografts of HER2-positive tumors. Results: The HER2-specific Affibody molecules were not toxic to HER2-overexpressing cells and their binding to HER2 did interfere with neither binding nor effectives of trastuzumab. The binding affinities and specificities of the Affibody-Alexa Fluor fluorescent conjugates to HER2 were unchanged or minimally affected by the modifications. Pharmacokinetics and biodistribution studies showed the albumin-binding domain-fused-(Z -Alexa Fluor 750 conjugate to be an optimal probe for optical imaging of HER2 in vivo. Conclusion: Our results suggest that Affibody-Alexa Fluor conjugates may be used as a specific NIR probe for the noninvasive semiquantitative imaging of HER2 expression in vivo. © 2008 American Association for Cancer Research.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=52449108735&origin=inward; http://dx.doi.org/10.1158/1078-0432.ccr-07-4076; http://www.ncbi.nlm.nih.gov/pubmed/18559604; http://clincancerres.aacrjournals.org/cgi/doi/10.1158/1078-0432.CCR-07-4076; https://syndication.highwire.org/content/doi/10.1158/1078-0432.CCR-07-4076; https://aacrjournals.org/clincancerres/article/14/12/3840/72680/Affibody-Molecules-for-In-vivo-Characterization-of; https://dx.doi.org/10.1158/1078-0432.ccr-07-4076; https://clincancerres.aacrjournals.org/content/14/12/3840
American Association for Cancer Research (AACR)
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