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<script type="text/javascript" src="/corehtml/pmc/jatsreader/ptpmc_3.22/js/jr.boots.min.js"> </script><title>4-[18F]Fluorobenzoyl-Phe-Ala-Leu-Gly-Glu-Ala-NH2 - Molecular Imaging and Contrast Agent Database (MICAD) - NCBI Bookshelf</title>
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<meta name="citation_inbook_title" content="Molecular Imaging and Contrast Agent Database (MICAD) [Internet]">
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<meta name="citation_title" content="4-[18F]Fluorobenzoyl-Phe-Ala-Leu-Gly-Glu-Ala-NH2">
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<meta name="citation_author" content="Kam Leung">
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<meta name="og:description" content="Epidermal growth factor (EGF) is a 53-amino-acid cytokine (6.2 kDa) secreted by ectodermic cells, monocytes, kidneys, and duodenal glands (1). EGF stimulates growth of epidermal and epithelial cells. EGF and at least seven other growth factors and their transmembrane receptor kinases play important roles in cell proliferation, survival, adhesion, migration, and differentiation. The EGF receptor (EGFR) family consists of four transmembrane receptors, including EGFR (HER1/erbB-1), HER2 (erbB-2/neu), HER3 (erbB-3), and HER4 (erbB-4) (2). HER1, HER3, and HER4 comprise three major functional domains: an extracellular ligand-binding domain, a hydrophobic transmembrane domain, and a cytoplasmic tyrosine kinase domain (2, 3). EGFR, which is overexpressed in many malignant epithelial tumors, contributes to gene amplification, which is believed to introduce mutations in the receptor (4). The overexpression, amplification, and/or mutation of EGFR can lead to the development of cancer. The most common mutation observed in the receptor is the deletion of a segment (amino acid residues 6–273 of the EGFR extracellular domain), including the ligand-binding region, which results in the generation of a variant known as constitutively activated variant III EGFR (EGFRvIII) (5). Although EGFRvIII is nonresponsive to EGF, it remains a constantly operating downstream tyrosine kinase signaling pathway that appears to promote the development of a neoplastic phenotype, particularly for glioblastoma and to some extent for other cancers such as those of the prostate and the breast (6). EGFRvIII has not been identified in normal tissues.">
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id="jr-fip-info-p"><a id="jr-fip-prev" class="wsprkl btn" title="Jump to previuos match">◀</a><button id="jr-fip-matches">no matches yet</button><a id="jr-fip-next" class="wsprkl btn" title="Jump to next match">▶</a></nav></nav></div><div id="jr-epub-interstitial" class="hidden"></div><div id="jr-content"><article data-type="main"><div class="main-content lit-style" itemscope="itemscope" itemtype="http://schema.org/CreativeWork"><div class="meta-content fm-sec"><div class="fm-sec"><h1 id="_NBK82507_"><span class="title" itemprop="name">4-[<sup>18</sup>F]Fluorobenzoyl-Phe-Ala-Leu-Gly-Glu-Ala-NH<sub>2</sub></span></h1><div itemprop="alternativeHeadline" class="subtitle whole_rhythm">[<sup>18</sup>F]FBA-FALGEA-NH<sub>2</sub></div><p class="contribs">Leung K.</p><p class="fm-aai"><a href="#_NBK82507_pubdet_">Publication Details</a></p></div></div><div class="jig-ncbiinpagenav body-content whole_rhythm" data-jigconfig="allHeadingLevels: ['h2'],smoothScroll: false" itemprop="text"><div class="iconblock whole_rhythm clearfix ten_col table-wrap" id="figFBAFALGEA18FTncchemicalname418fflu"><a href="/books/NBK82507/table/FBA-FALGEA-18F.T.nc_chemical_name418fflu/?report=objectonly" target="object" title="Table" class="img_link icnblk_img figpopup" rid-figpopup="figFBAFALGEA18FTncchemicalname418fflu" rid-ob="figobFBAFALGEA18FTncchemicalname418fflu"><img class="small-thumb" src="/books/NBK82507/table/FBA-FALGEA-18F.T.nc_chemical_name418fflu/?report=thumb" src-large="/books/NBK82507/table/FBA-FALGEA-18F.T.nc_chemical_name418fflu/?report=previmg" alt="Image " /></a><div class="icnblk_cntnt"><h4 id="FBA-FALGEA-18F.T.nc_chemical_name418fflu"><a href="/books/NBK82507/table/FBA-FALGEA-18F.T.nc_chemical_name418fflu/?report=objectonly" target="object" rid-ob="figobFBAFALGEA18FTncchemicalname418fflu">Table</a></h4><p class="float-caption no_bottom_margin">
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<i>In vitro</i>
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Rodents
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</p></div></div><div id="FBA-FALGEA-18F.Background"><h2 id="_FBA-FALGEA-18F_Background_">Background</h2><p>[<a href="/pubmed?term=FALGEA&cmd=DetailsSearch" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>Epidermal growth factor (EGF) is a 53-amino-acid cytokine (6.2 kDa) secreted by ectodermic cells, monocytes, kidneys, and duodenal glands (<a class="bibr" href="#FBA-FALGEA-18F.REF.1" rid="FBA-FALGEA-18F.REF.1">1</a>). EGF stimulates growth of epidermal and epithelial cells. EGF and at least seven other growth factors and their transmembrane receptor kinases play important roles in cell proliferation, survival, adhesion, migration, and differentiation. The EGF receptor (EGFR) family consists of four transmembrane receptors, including EGFR (HER1/erbB-1), HER2 (erbB-2/neu), HER3 (erbB-3), and HER4 (erbB-4) (<a class="bibr" href="#FBA-FALGEA-18F.REF.2" rid="FBA-FALGEA-18F.REF.2">2</a>). HER1, HER3, and HER4 comprise three major functional domains: an extracellular ligand-binding domain, a hydrophobic transmembrane domain, and a cytoplasmic tyrosine kinase domain (<a class="bibr" href="#FBA-FALGEA-18F.REF.2" rid="FBA-FALGEA-18F.REF.2 FBA-FALGEA-18F.REF.3">2, 3</a>). EGFR, which is overexpressed in many malignant epithelial tumors, contributes to gene amplification, which is believed to introduce mutations in the receptor (<a class="bibr" href="#FBA-FALGEA-18F.REF.4" rid="FBA-FALGEA-18F.REF.4">4</a>). The overexpression, amplification, and/or mutation of EGFR can lead to the development of cancer. The most common mutation observed in the receptor is the deletion of a segment (amino acid residues 6–273 of the EGFR extracellular domain), including the ligand-binding region, which results in the generation of a variant known as constitutively activated variant III EGFR (EGFRvIII) (<a class="bibr" href="#FBA-FALGEA-18F.REF.5" rid="FBA-FALGEA-18F.REF.5">5</a>). Although EGFRvIII is nonresponsive to EGF, it remains a constantly operating downstream tyrosine kinase signaling pathway that appears to promote the development of a neoplastic phenotype, particularly for glioblastoma and to some extent for other cancers such as those of the prostate and the breast (<a class="bibr" href="#FBA-FALGEA-18F.REF.6" rid="FBA-FALGEA-18F.REF.6">6</a>). EGFRvIII has not been identified in normal tissues.</p><p>Monoclonal antibody (mAb) 806 and chimeric antibody ch806 (<a class="bibr" href="#FBA-FALGEA-18F.REF.7" rid="FBA-FALGEA-18F.REF.7 FBA-FALGEA-18F.REF.8">7, 8</a>), which specifically target EGFRvIII, were radiolabeled for imaging EGFRvIII expression in tumors. However, the pharmacokinetics of the intact radiolabeled mAb, with high liver uptake and slow blood elimination, are generally not ideal for imaging because of poor tissue and tumor penetration (<a class="bibr" href="#FBA-FALGEA-18F.REF.9" rid="FBA-FALGEA-18F.REF.9">9</a>). Smaller antibody fragments and peptides have better imaging pharmacokinetics because they are rapidly excreted by the kidneys. Denholt et al. (<a class="bibr" href="#FBA-FALGEA-18F.REF.10" rid="FBA-FALGEA-18F.REF.10">10</a>) identified an EGFRvIII-targeting peptide, H-Phe-Ala-Leu-Gly-Glu-Ala-NH<sub>2</sub> (H-FALGEA-NH<sub>2</sub>) using a Positional Scanning Synthetic Combinatorial Library. H-FALGEA-NH<sub>2</sub> was labeled with 4-[<sup>18</sup>F]fluorobenzoic acid ([<sup>18</sup>F]FBA) to form [<sup>18</sup>F]FBA-FALGEA-NH<sub>2</sub> (<a class="bibr" href="#FBA-FALGEA-18F.REF.11" rid="FBA-FALGEA-18F.REF.11">11</a>). [<sup>18</sup>F]FBA-FALGEA-NH<sub>2</sub> has been evaluated for imaging of EGFRvIII expression in human glioblastoma multiforme (GBM) tumors in nude mice using positron emission tomography (PET).</p><div id="FBA-FALGEA-18F.Related_Resource_Links"><h3>Related Resource Links:</h3><ul><li class="half_rhythm"><div>Chapters in MICAD (<a href="/sites/entrez?db=Books&cmd=Search&term=EGFR+AND+micad%5bbook%5d&doptcmdl=TOCView&log%24=booksrch&bname=micad" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">EGFR</a>, <a href="/books?term=EGFRvIII%20AND%20micad%5Bbook%5D" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">EGFRvIII</a>)</div></li><li class="half_rhythm"><div>Gene information in NCBI (<a href="/gene/1956" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">EGFR</a>)</div></li><li class="half_rhythm"><div>Articles in Online Mendelian Inheritance in Man (OMIM) (<a href="/omim/131550" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">EGFR</a>)</div></li><li class="half_rhythm"><div>Clinical trials (<a href="http://www.clinicaltrials.gov/ct2/results?term=EGFRvIII" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">EGFRvIII</a>)</div></li><li class="half_rhythm"><div>Drug information in FDA (<a href="http://google2.fda.gov/search?q=EGFRvIII&client=FDAgov&site=FDAgov&lr=&proxystylesheet=FDAgov&output=xml_no_dtd&getfields=*&x=8&y=12" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">EGFRvIII</a>)</div></li></ul></div></div><div id="FBA-FALGEA-18F.Synthesis"><h2 id="_FBA-FALGEA-18F_Synthesis_">Synthesis</h2><p>[<a href="/pubmed?term=FALGEA%20synthesis&cmd=DetailsSearch" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p> [<sup>18</sup>F]FBA was synthesized in two steps from [<sup>18</sup>F]KF (Kryptofix 2.2.2./K<sub>2</sub>CO<sub>3</sub>) (<a class="bibr" href="#FBA-FALGEA-18F.REF.11" rid="FBA-FALGEA-18F.REF.11">11</a>). The decay-corrected yields of [<sup>18</sup>F]FBA were 22%–54%, based on starting with [<sup>18</sup>F]KF. H-FALGEA-XAL-resin and 250–500 MBq (6.8–13.5 mCi) [<sup>18</sup>F]FBA were incubated for 30 min at room temperature. [<sup>18</sup>F]FBA-FALGEA-NH<sub>2</sub> was cleaved from the resin by heating with trifluoroacetic acid for 20 min at 35°C. Total synthesis time was ~180 min, including the final high-performance liquid chromatography (HPLC) purification. The decay-corrected radiochemical yields, radiochemical purity, and specific activity of [<sup>18</sup>F]FBA-FALGEA-NH<sub>2</sub> were 7.3 ± 1.1%, 95 ± 3%, and 6.4 ± 1.1 GBq/µmol (170 ± 30 mCi/µmol) (<i>n</i> = 6), respectively, at the end of HPLC purification.</p></div><div id="FBA-FALGEA-18F.In_Vitro_Studies_Testing"><h2 id="_FBA-FALGEA-18F_In_Vitro_Studies_Testing_"><i>In Vitro</i> Studies: Testing in Cells and Tissues</h2><p>[<a href="/pubmed?term=FALGEA%20in%20vitro&cmd=DetailsSearch" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>The binding affinity (<i>K</i><sub>d</sub>) values of [<sup>18</sup>F]FBA-FALGEA-NH<sub>2</sub> to NR6M cells (expressing EGFRvIII) and NR6W-A cells (expressing EGFR) were reported to be 23 nM and 691 nM (<a class="bibr" href="#FBA-FALGEA-18F.REF.11" rid="FBA-FALGEA-18F.REF.11">11</a>), respectively. The <i>B</i><sub>max</sub> (receptor density) values for EGFRvIII and EGFR were reported to be 77 pmol × 10<sup>3</sup> cells and 596 nmol × 10<sup>3</sup> cells, respectively. The <i>in vitro</i> stability of [<sup>18</sup>F]FBA-FALGEA-NH<sub>2</sub> in nude mouse plasma was 85% and 53% intact after 30 min and 60 min of incubation, respectively.</p></div><div id="FBA-FALGEA-18F.Animal_Studies"><h2 id="_FBA-FALGEA-18F_Animal_Studies_">Animal Studies</h2><div id="FBA-FALGEA-18F.Rodents"><h3>Rodents</h3><p>[<a href="/pubmed?term=FALGEA%20rodentia&cmd=DetailsSearch" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>Denholt et al. (<a class="bibr" href="#FBA-FALGEA-18F.REF.11" rid="FBA-FALGEA-18F.REF.11">11</a>) performed PET imaging studies in nude mice bearing EGFRvIII-expressing human GBM tumors (7 mice, 11 tumors) and nude mice bearing EGFRvIII non-expressing human GBM tumors (5 mice, 10 tumors) at 60 min after injection of 5.7 ± 2.5 MBq (0.15 ± 0.7 mCi) [<sup>18</sup>F]FBA-FALGEA-NH<sub>2</sub>. The EGFRvIII-positive tumors were clearly visualized compared to the control tumors. The tumor/muscle ratios for EGFRvIII-positive tumors and control tumors were 7.8 ± 3.2 and 3.4 ± 1.0, respectively. The average standard uptake value (SUV = Tissue concentration/(injected dose/body weight)) of 0.11 was low for the EGFRvIII-positive tumors. The liver and kidneys were also visualized in both groups of tumor-bearing mice with higher radioactivity in the kidneys. There was a linear correlation between tumor/muscle ratios and EGFRvIII mRNA expression on the tumors (<i>R</i> = 0.86, <i>P</i> < 0.007). No blocking studies were performed. Furthermore, no intact [<sup>18</sup>F]FBA-FALGEA-NH<sub>2</sub> was detected in the plasma at 5 min after injection, indicating rapid metabolism by blood peptidases. In comparison, [<sup>18</sup>F]FDG PET studies were performed one day before [<sup>18</sup>F]FBA-FALGEA-NH<sub>2</sub> PET studies in the same nude mice bearing EGFRvIII tumors. The tumor/muscle ratio was 2.6 with an average SUV of 0.54 at 60 min after injection. The investigators concluded that a more stable peptide with higher affinity for EGFRvIII is needed to decrease the large variation in binding of [<sup>18</sup>F]FBA-FALGEA-NH<sub>2</sub> to EGFRvIII-positive tumors.</p></div><div id="FBA-FALGEA-18F.Other_NonPrimate_Mammals"><h3>Other Non-Primate Mammals</h3><p>[<a href="/pubmed?term=FALGEA%20Non-Primate%20Mammals&cmd=DetailsSearch" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>No references are currently available.</p></div><div id="FBA-FALGEA-18F.NonHuman_Primates"><h3>Non-Human Primates</h3><p>[<a href="/pubmed?term=FALGEA%20Non-Human%20Primates&cmd=DetailsSearch" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>No references are currently available.</p></div></div><div id="FBA-FALGEA-18F.Human_Studies"><h2 id="_FBA-FALGEA-18F_Human_Studies_">Human Studies</h2><p>[<a href="/pubmed?term=FALGEA%20Human%20Studies&cmd=DetailsSearch" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>No references are currently available.</p></div><div id="FBA-FALGEA-18F.References"><h2 id="_FBA-FALGEA-18F_References_">References</h2><dl class="temp-labeled-list"><dl class="bkr_refwrap"><dt>1.</dt><dd><div class="bk_ref" id="FBA-FALGEA-18F.REF.1">Carpenter G., Cohen S.
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<em>Epidermal growth factor.</em>
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<span><span class="ref-journal">J Biol Chem. </span>1990;<span class="ref-vol">265</span>(14):7709–12.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/2186024" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 2186024</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>2.</dt><dd><div class="bk_ref" id="FBA-FALGEA-18F.REF.2">Spector N.L., Blackwell K.L.
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<em>Understanding the mechanisms behind trastuzumab therapy for human epidermal growth factor receptor 2-positive breast cancer.</em>
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<span><span class="ref-journal">J Clin Oncol. </span>2009;<span class="ref-vol">27</span>(34):5838–47.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/19884552" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 19884552</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>3.</dt><dd><div class="bk_ref" id="FBA-FALGEA-18F.REF.3">Pines G., Kostler W.J., Yarden Y.
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<em>Oncogenic mutant forms of EGFR: lessons in signal transduction and targets for cancer therapy.</em>
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<span><span class="ref-journal">FEBS Lett. </span>2010;<span class="ref-vol">584</span>(12):2699–706.</span> [<a href="/pmc/articles/PMC2892754/" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pmc">PMC free article<span class="bk_prnt">: PMC2892754</span></a>] [<a href="https://pubmed.ncbi.nlm.nih.gov/20388509" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 20388509</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>4.</dt><dd><div class="bk_ref" id="FBA-FALGEA-18F.REF.4">Scott A.M., Lee F.T., Tebbutt N., Herbertson R., Gill S.S., Liu Z., Skrinos E., Murone C., Saunder T.H., Chappell B., Papenfuss A.T., Poon A.M., Hopkins W., Smyth F.E., MacGregor D., Cher L.M., Jungbluth A.A., Ritter G., Brechbiel M.W., Murphy R., Burgess A.W., Hoffman E.W., Johns T.G., Old L.J.
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<em>A phase I clinical trial with monoclonal antibody ch806 targeting transitional state and mutant epidermal growth factor receptors.</em>
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<span><span class="ref-journal">Proc Natl Acad Sci U S A. </span>2007;<span class="ref-vol">104</span>(10):4071–6.</span> [<a href="/pmc/articles/PMC1805701/" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pmc">PMC free article<span class="bk_prnt">: PMC1805701</span></a>] [<a href="https://pubmed.ncbi.nlm.nih.gov/17360479" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 17360479</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>5.</dt><dd><div class="bk_ref" id="FBA-FALGEA-18F.REF.5">Gan H.K., Kaye A.H., Luwor R.B.
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<em>The EGFRvIII variant in glioblastoma multiforme.</em>
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<span><span class="ref-journal">J Clin Neurosci. </span>2009;<span class="ref-vol">16</span>(6):748–54.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/19324552" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 19324552</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>6.</dt><dd><div class="bk_ref" id="FBA-FALGEA-18F.REF.6">Lee F.T., O'Keefe G.J., Gan H.K., Mountain A.J., Jones G.R., Saunder T.H., Sagona J., Rigopoulos A., Smyth F.E., Johns T.G., Govindan S.V., Goldenberg D.M., Old L.J., Scott A.M.
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<em>Immuno-PET quantitation of de2-7 epidermal growth factor receptor expression in glioma using 124I-IMP-R4-labeled antibody ch806.</em>
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<span><span class="ref-journal">J Nucl Med. </span>2010;<span class="ref-vol">51</span>(6):967–72.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/20484439" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 20484439</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>7.</dt><dd><div class="bk_ref" id="FBA-FALGEA-18F.REF.7">Jungbluth A.A., Stockert E., Huang H.J., Collins V.P., Coplan K., Iversen K., Kolb D., Johns T.J., Scott A.M., Gullick W.J., Ritter G., Cohen L., Scanlan M.J., Cavenee W.K., Old L.J.
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<em>A monoclonal antibody recognizing human cancers with amplification/overexpression of the human epidermal growth factor receptor.</em>
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<span><span class="ref-journal">Proc Natl Acad Sci U S A. </span>2003;<span class="ref-vol">100</span>(2):639–44.</span> [<a href="/pmc/articles/PMC141049/" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pmc">PMC free article<span class="bk_prnt">: PMC141049</span></a>] [<a href="https://pubmed.ncbi.nlm.nih.gov/12515857" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 12515857</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>8.</dt><dd><div class="bk_ref" id="FBA-FALGEA-18F.REF.8">Perera R.M., Zoncu R., Johns T.G., Pypaert M., Lee F.T., Mellman I., Old L.J., Toomre D.K., Scott A.M.
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<em>Internalization, intracellular trafficking, and biodistribution of monoclonal antibody 806: a novel anti-epidermal growth factor receptor antibody.</em>
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<span><span class="ref-journal">Neoplasia. </span>2007;<span class="ref-vol">9</span>(12):1099–110.</span> [<a href="/pmc/articles/PMC2134906/" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pmc">PMC free article<span class="bk_prnt">: PMC2134906</span></a>] [<a href="https://pubmed.ncbi.nlm.nih.gov/18084617" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 18084617</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>9.</dt><dd><div class="bk_ref" id="FBA-FALGEA-18F.REF.9">McGregor D.P.
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<em>Discovering and improving novel peptide therapeutics.</em>
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<span><span class="ref-journal">Curr Opin Pharmacol. </span>2008;<span class="ref-vol">8</span>(5):616–9.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/18602024" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 18602024</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>10.</dt><dd><div class="bk_ref" id="FBA-FALGEA-18F.REF.10">Denholt C.L., Hansen P.R., Pedersen N., Poulsen H.S., Gillings N., Kjaer A.
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<em>Identification of novel peptide ligands for the cancer-specific receptor mutation EFGRvIII using a mixture-based synthetic combinatorial library.</em>
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<span><span class="ref-journal">Biopolymers. </span>2009;<span class="ref-vol">91</span>(3):201–6.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/19107925" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 19107925</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>11.</dt><dd><div class="bk_ref" id="FBA-FALGEA-18F.REF.11">Denholt C.L., Binderup T., Stockhausen M.T., Poulsen H.S., Spang-Thomsen M., Hansen P.R., Gillings N., Kjaer A.
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<em>Evaluation of 4-[18F]fluorobenzoyl-FALGEA-NH2 as a positron emission tomography tracer for epidermal growth factor receptor mutation variant III imaging in cancer.</em>
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<span><span class="ref-journal">Nucl Med Biol. </span>2011;<span class="ref-vol">38</span>(4):509–15.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/21531288" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 21531288</span></a>]</div></dd></dl></dl></div><div id="bk_toc_contnr"></div></div></div><div class="fm-sec"><h2 id="_NBK82507_pubdet_">Publication Details</h2><h3>Author Information and Affiliations</h3><div class="contrib half_rhythm"><span itemprop="author">Kam Leung</span>, PhD<div class="affiliation small">National Center for Biotechnology Information, NLM, NIH, Bethesda, MD<div><span class="email-label">Email: </span><a href="mailto:dev@null" data-email="vog.hin.mln.ibcn@dacim" class="oemail">vog.hin.mln.ibcn@dacim</a></div></div></div><h3>Publication History</h3><p class="small">Created: <span itemprop="datePublished">August 26, 2011</span>; Last Update: <span itemprop="dateModified">December 8, 2011</span>.</p><h3>Copyright</h3><div><div class="half_rhythm"><a href="/books/about/copyright/">Copyright Notice</a></div></div><h3>Publisher</h3><p><a href="http://www.ncbi.nlm.nih.gov/" ref="pagearea=page-banner&targetsite=external&targetcat=link&targettype=publisher">National Center for Biotechnology Information (US)</a>, Bethesda (MD)</p><h3>NLM Citation</h3><p>Leung K. 4-[18F]Fluorobenzoyl-Phe-Ala-Leu-Gly-Glu-Ala-NH2. 2011 Aug 26 [Updated 2011 Dec 8]. In: Molecular Imaging and Contrast Agent Database (MICAD) [Internet]. Bethesda (MD): National Center for Biotechnology Information (US); 2004-2013. <span class="bk_cite_avail"></span></p></div><div class="small-screen-prev"><a href="/books/n/micad/A20FMDV2-18F/?report=reader"><svg xmlns="http://www.w3.org/2000/svg" viewBox="0 0 100 100" preserveAspectRatio="none"><path d="M75,30 c-80,60 -80,0 0,60 c-30,-60 -30,0 0,-60"></path><text x="20" y="28" textLength="60" style="font-size:25px">Prev</text></svg></a></div><div class="small-screen-next"><a href="/books/n/micad/FB-RMSH-18F/?report=reader"><svg xmlns="http://www.w3.org/2000/svg" viewBox="0 0 100 100" preserveAspectRatio="none"><path d="M25,30c80,60 80,0 0,60 c30,-60 30,0 0,-60"></path><text x="20" y="28" textLength="60" style="font-size:25px">Next</text></svg></a></div></article><article data-type="table-wrap" id="figobFBAFALGEA18FTncchemicalname418fflu"><div id="FBA-FALGEA-18F.T.nc_chemical_name418fflu" class="table"><p class="large-table-link" style="display:none"><span class="right"><a href="/books/NBK82507/table/FBA-FALGEA-18F.T.nc_chemical_name418fflu/?report=objectonly" target="object">View in own window</a></span></p><div class="large_tbl" id="__FBA-FALGEA-18F.T.nc_chemical_name418fflu_lrgtbl__"><table><tbody><tr><td rowspan="1" colspan="1" style="text-align:right;vertical-align:top;">
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<b>Chemical name:</b>
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</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;">4-[<sup>18</sup>F]Fluorobenzoyl-Phe-Ala-Leu-Gly-Glu-Ala-NH<sub>2</sub></td><td rowspan="9" colspan="1" style="text-align:center;vertical-align:middle;"></td></tr><tr><td rowspan="1" colspan="1" style="text-align:right;vertical-align:top;">
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<b>Abbreviated name:</b>
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</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;">[<sup>18</sup>F]FBA-FALGEA-NH<sub>2</sub></td></tr><tr><td rowspan="1" colspan="1" style="text-align:right;vertical-align:top;">
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<b>Synonym:</b>
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</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;">[<sup>18</sup>F]FB-FALGEA-NH<sub>2</sub></td></tr><tr><td rowspan="1" colspan="1" style="text-align:right;vertical-align:top;">
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<b>Agent Category:</b>
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</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;">Peptide</td></tr><tr><td rowspan="1" colspan="1" style="text-align:right;vertical-align:top;">
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<b>Target:</b>
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</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;">Epidermal growth factor receptor variant III (EGFRvIII)<br /></td></tr><tr><td rowspan="1" colspan="1" style="text-align:right;vertical-align:top;">
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<b>Target Category:</b>
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</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;">Receptor</td></tr><tr><td rowspan="1" colspan="1" style="text-align:right;vertical-align:top;">
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<b>Method of detection:</b>
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</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;">Positron emission tomography (PET)</td></tr><tr><td rowspan="1" colspan="1" style="text-align:right;vertical-align:top;">
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<b>Source of signal / contrast:</b>
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</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;"><sup>18</sup>F</td></tr><tr><td rowspan="1" colspan="1" style="text-align:right;vertical-align:top;">
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<b>Activation:</b>
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</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;">No</td></tr><tr><td rowspan="1" colspan="1" style="text-align:right;vertical-align:top;">
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<b>Studies:</b>
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</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;">
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<ul class="simple-list"><li class="half_rhythm"><div>
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<img alt="Checkbox" src="/corehtml/pmc/css/bookshelf/2.26/img/studies.checkbox.png" />
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<i>In vitro</i>
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</div></li><li class="half_rhythm"><div>
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<img alt="Checkbox" src="/corehtml/pmc/css/bookshelf/2.26/img/studies.checkbox.png" /> Rodents
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</div></li></ul>
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</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;">Structure not available in <a href="http://pubchem.ncbi.nlm.nih.gov/" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubChem</a>.</td></tr></tbody></table></div></div></article></div><div id="jr-scripts"><script src="/corehtml/pmc/jatsreader/ptpmc_3.22/js/libs.min.js"> </script><script src="/corehtml/pmc/jatsreader/ptpmc_3.22/js/jr.min.js"> </script></div></div>
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