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<script type="text/javascript" src="/corehtml/pmc/jatsreader/ptpmc_3.22/js/jr.boots.min.js"> </script><title>Cy7-Tyr-d-Glu-Cys-Hyp-Tyr(3-Cl)-Gly-Leu-Cys-Tyr-Ile-Gln-NH2 - Molecular Imaging and Contrast Agent Database (MICAD) - NCBI Bookshelf</title>
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<meta name="citation_title" content="Cy7-Tyr-d-Glu-Cys-Hyp-Tyr(3-Cl)-Gly-Leu-Cys-Tyr-Ile-Gln-NH2">
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<meta name="citation_date" content="2013/05/30">
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<meta name="citation_author" content="Kam Leung">
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<meta name="og:description" content="Optical fluorescence imaging is increasingly used to monitor biological functions of specific targets in small animals (1-4). However, the intrinsic fluorescence of biomolecules poses a problem when fluorophores that absorb visible light (350–650 nm) are used. Near-infrared (NIR) fluorescence (650–1,000 nm) detection avoids the natural background fluorescence interference of biomolecules, providing a high contrast between target and background tissues in small animals. NIR fluorophores have a wider dynamic range and minimal background fluorescence as a result of reduced scattering compared with visible fluorescence detection. NIR fluorophores also have high sensitivity, attributable to low background fluorescence, and high extinction coefficients, which provide high quantum yields. The NIR region is also compatible with solid-state optical components, such as diode lasers and silicon detectors. NIR fluorescence imaging is a noninvasive alternative to radionuclide imaging in small animals (4, 5).">
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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="_NBK138567_"><span class="title" itemprop="name">Cy7-Tyr-<span class="small-caps">d</span>-Glu-Cys-Hyp-Tyr(3-Cl)-Gly-Leu-Cys-Tyr-Ile-Gln-NH<sub>2</sub></span></h1><div itemprop="alternativeHeadline" class="subtitle whole_rhythm">Cy7-FTP11</div><p class="contribs">Leung K.</p><p class="fm-aai"><a href="#_NBK138567_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="figFTP11Cy7Tncchemicalnamecy7tyrdglucy"><a href="/books/NBK138567/table/FTP11-Cy7.T.nc_chemical_namecy7tyrdglucy/?report=objectonly" target="object" title="Table" class="img_link icnblk_img" rid-ob="figobFTP11Cy7Tncchemicalnamecy7tyrdglucy"><img class="small-thumb" src="/corehtml/pmc/css/bookshelf/2.26/img/table-icon.gif" alt="Table Icon" /></a><div class="icnblk_cntnt"><h4 id="FTP11-Cy7.T.nc_chemical_namecy7tyrdglucy"><a href="/books/NBK138567/table/FTP11-Cy7.T.nc_chemical_namecy7tyrdglucy/?report=objectonly" target="object" rid-ob="figobFTP11Cy7Tncchemicalnamecy7tyrdglucy">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="FTP11-Cy7.Background"><h2 id="_FTP11-Cy7_Background_">Background</h2><p>[<a href="/sites/entrez?Db=pubmed&Cmd=DetailsSearch&Term=FTP11" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>Optical fluorescence imaging is increasingly used to monitor biological functions of specific targets in small animals (<a class="bibr" href="#FTP11-Cy7.REF.1" rid="FTP11-Cy7.REF.1 FTP11-Cy7.REF.2 FTP11-Cy7.REF.3 FTP11-Cy7.REF.4">1-4</a>). However, the intrinsic fluorescence of biomolecules poses a problem when fluorophores that absorb visible light (350–650 nm) are used. Near-infrared (NIR) fluorescence (650–1,000 nm) detection avoids the natural background fluorescence interference of biomolecules, providing a high contrast between target and background tissues in small animals. NIR fluorophores have a wider dynamic range and minimal background fluorescence as a result of reduced scattering compared with visible fluorescence detection. NIR fluorophores also have high sensitivity, attributable to low background fluorescence, and high extinction coefficients, which provide high quantum yields. The NIR region is also compatible with solid-state optical components, such as diode lasers and silicon detectors. NIR fluorescence imaging is a noninvasive alternative to radionuclide imaging in small animals (<a class="bibr" href="#FTP11-Cy7.REF.4" rid="FTP11-Cy7.REF.4 FTP11-Cy7.REF.5">4, 5</a>).</p><p>Extracellular matrix adhesion molecules consist of a complex network of fibronectins, collagens, chondroitins, laminins, glycoproteins, heparin sulfate, tenascins, and proteoglycans that surround connective tissue cells, and they are mainly secreted by fibroblasts, chondroblasts, and osteoblasts (<a class="bibr" href="#FTP11-Cy7.REF.6" rid="FTP11-Cy7.REF.6">6</a>). Cell substrate adhesion molecules are considered essential regulators of cell migration, differentiation, and tissue integrity and remodeling. These molecules play a role in inflammation and atherogenesis, but they also participate in the process of invasion and metastasis of malignant cells in the host tissue (<a class="bibr" href="#FTP11-Cy7.REF.7" rid="FTP11-Cy7.REF.7">7</a>). A meshwork of clotted plasma protein was present in the tumor stroma but not in normal tissues, providing a functional matrix for angiogenesis, cell migration, and tumor cell invasion (<a class="bibr" href="#FTP11-Cy7.REF.8" rid="FTP11-Cy7.REF.8">8</a>). There are high levels of collagens, fibronectin, and fibrin in the tumor connective tissues.</p><p>Thrombosis plays a major role in many cardiovascular diseases such as myocardial infarction, pulmonary embolism, deep venous thrombosis, and cerebral venous thrombosis (<a class="bibr" href="#FTP11-Cy7.REF.9" rid="FTP11-Cy7.REF.9">9</a>). Thrombosis occurs by an activation process of thrombin (F2 coagulation factor II), which then converts fibrinogen into fibrin. Thrombin initiates the cross-linking of the polymerized fibrin <i>via</i> the activation of a transglutamase enzyme called coagulation factor XIII (FXIIIa indicates activated factor XIII) (<a class="bibr" href="#FTP11-Cy7.REF.10" rid="FTP11-Cy7.REF.10">10</a>). Atherosclerotic lesions often contain microthrombi and fibrin on their surface. Fibrin is associated with a variety of malignant tumors. Fibrin is essential for stroma formation in the tumor with deposition of fibrin, which leads to tumor angiogenesis and metastasis. Hara et al. (<a class="bibr" href="#FTP11-Cy7.REF.11" rid="FTP11-Cy7.REF.11">11</a>) prepared Cy7-Tyr-<span class="small-caps">d</span>-Glu-Cys-Hyp-Tyr(3-Cl)-Gly-Leu-Cys-Tyr-Ile-Gln-NH<sub>2</sub> (Cy7-FTP11) for use with NIR fluorescence imaging of fibrin in thrombi in mice using high-resolution intravital fluorescence microscopy and fluorescence molecular tomography.</p><div id="FTP11-Cy7.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=fibrin+AND+micad%5bbook%5d&doptcmdl=TOCView&log%24=booksrch&bname=micad" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">fibrin</a>)</div></li><li class="half_rhythm"><div>Gene information in NCBI (<a href="/gene/2243" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">fibrinogen</a>, <a href="/gene/2335" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">fibronectin</a>)</div></li><li class="half_rhythm"><div>Articles in Online Mendelian Inheritance in Man (OMIM) (<a href="/omim/134820" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">fibrinogen</a>, <a href="http://omim.org/entry/135600" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">fibronectin</a>)</div></li></ul></div></div><div id="FTP11-Cy7.Synthesis"><h2 id="_FTP11-Cy7_Synthesis_">Synthesis</h2><p>[<a href="/sites/entrez?Db=pubmed&Cmd=DetailsSearch&Term=FTP11+synthesis" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>FTP11 was synthesized with solid-phase peptide synthesis (<a class="bibr" href="#FTP11-Cy7.REF.11" rid="FTP11-Cy7.REF.11">11</a>). Cy7 was conjugated to the N-terminal amino group of FTP11 with addition of Cy7-succinimidyl ester. Cy7-FTP11 was isolated with high-performance liquid chromatography and cyclized by oxidation in dimethyl sulfoxide with >98% purity. Cy7-FTP11 exhibited an expected molecular mass of 2.62 kDa using matrix-assisted laser desorption/ionization mass spectrometry.</p></div><div id="FTP11-Cy7.In_Vitro_Studies_Testing_in_Ce"><h2 id="_FTP11-Cy7_In_Vitro_Studies_Testing_in_Ce_"><i>In Vitro</i> Studies: Testing in Cells and Tissues</h2><p>[<a href="/sites/entrez?Db=pubmed&Cmd=DetailsSearch&Term=FTP11+in+vitro" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p><i>In vitro</i> fluorescence reflective imaging studies showed that Cy7-FTP11 exhibited significantly higher (<i>P</i> < 0.0001) target/background ratios (TBR) than free Cy7 to fibrin in human plasma clots, with TBRs of 6.30 ± 0.34 and 1.20 ± 0.03 (<a class="bibr" href="#FTP11-Cy7.REF.11" rid="FTP11-Cy7.REF.11">11</a>), respectively. Excess unlabeled FTP11 (100-fold) inhibited the TBR of Cy7-FTP11 to 2.50 ± 0.34 (<i>P</i> < 0.05).</p></div><div id="FTP11-Cy7.Animal_Studies"><h2 id="_FTP11-Cy7_Animal_Studies_">Animal Studies</h2><div id="FTP11-Cy7.Rodents"><h3>Rodents</h3><p>[<a href="/sites/entrez?Db=pubmed&Cmd=DetailsSearch&Term=FTP11+rodentia" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>Intravital fluorescence microscopy imaging studies were performed in mice (<i>n</i> = 5/group) with the femoral vein exposed and treated with 7.5% FeCl<sub>3</sub> solution to induce acute (2 h) and sub-acute (72 h) thrombosis (<a class="bibr" href="#FTP11-Cy7.REF.11" rid="FTP11-Cy7.REF.11">11</a>). Cy7 or Cy7-FTP11 (150 nmol/kg) was injected <i>via</i> retro-orbital administration. NIR fluorescence signal (TBRs) increased in both acute (3.5 ± 0.3) and sub-acute (2.7 ± 05) thrombi at 60 min after injection of Cy7-FTP11, whereas no increase was observed with Cy7 (0.46 ± 0.08). Blocking studies were performed in mice (<i>n</i> = 4/group) with acute thrombosis after pretreatment with 100-fold excess unlabeled FTP11 (1,500 nmol/kg) 30 min before Cy7-FTP11 (15 nmol/kg) injection. Thrombus TBR at 60 min decreased from 1.60 ± 0.11 to 0.99 ± 0.04 (<i>P</i> < 0.01). Histostaining of the veins confirmed the localization of NIR fluorescence signals in the thrombi. Cy7-FTP11 exhibited a blood half-life of 2.82 min (<i>n</i> = 5).</p><p>Noninvasive fluorescence molecular tomography imaging studies were performed in mice with the left jugular vein treated with 7.5% FeCl<sub>3</sub> solution to induce sub-acute thrombosis (<a class="bibr" href="#FTP11-Cy7.REF.11" rid="FTP11-Cy7.REF.11">11</a>). The contralateral right jugular vein was sham-operated. FMT signals from jugular veins were co-registered with anatomic computed tomography images. The TBR of the left jugular vein thrombi (3.5 ± 0.7) was 1.3-fold higher than that of the contralateral right jugular vein (1.5 ± 0.3) (<i>P</i> < 0.05). <i>Ex vivo</i> NIR fluorescence signals were 3.9 ± 0.4 and 2.4 ± 0.4 (<i>P</i> < 0.05) for the left and right jugular veins, respectively.</p></div><div id="FTP11-Cy7.Other_NonPrimate_Mammals"><h3>Other Non-Primate Mammals</h3><p>[<a href="/sites/entrez?Db=pubmed&Cmd=DetailsSearch&Term=FTP11+(dog+or+pig+or+sheep+or+rabbit)" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>No publication is currently available.</p></div><div id="FTP11-Cy7.NonHuman_Primates"><h3>Non-Human Primates</h3><p>[<a href="/sites/entrez?Db=pubmed&Cmd=DetailsSearch&Term=FTP11+(primate+not+human)" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>No publication is currently available.</p></div></div><div id="FTP11-Cy7.Human_Studies"><h2 id="_FTP11-Cy7_Human_Studies_">Human Studies</h2><p>[<a href="/sites/entrez?Db=pubmed&Cmd=DetailsSearch&Term=FTP11+human" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>No publication is currently available.</p></div><div id="FTP11-Cy7.References"><h2 id="_FTP11-Cy7_References_">References</h2><dl class="temp-labeled-list"><dl class="bkr_refwrap"><dt>1.</dt><dd><div class="bk_ref" id="FTP11-Cy7.REF.1">Achilefu S.
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<em>Lighting up tumors with receptor-specific optical molecular probes.</em>
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<span><span class="ref-journal">Technol Cancer Res Treat. </span>2004;<span class="ref-vol">3</span>(4):393–409.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/15270591" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 15270591</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>2.</dt><dd><div class="bk_ref" id="FTP11-Cy7.REF.2">Ntziachristos V., Bremer C., Weissleder R.
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<em>Fluorescence imaging with near-infrared light: new technological advances that enable in vivo molecular imaging.</em>
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<span><span class="ref-journal">Eur Radiol. </span>2003;<span class="ref-vol">13</span>(1):195–208.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/12541130" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 12541130</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>3.</dt><dd><div class="bk_ref" id="FTP11-Cy7.REF.3">Becker A., Hessenius C., Licha K., Ebert B., Sukowski U., Semmler W., Wiedenmann B., Grotzinger C.
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<em>Receptor-targeted optical imaging of tumors with near-infrared fluorescent ligands.</em>
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<span><span class="ref-journal">Nat Biotechnol. </span>2001;<span class="ref-vol">19</span>(4):327–31.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/11283589" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 11283589</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>4.</dt><dd><div class="bk_ref" id="FTP11-Cy7.REF.4">Leung K., Chopra A., Shan L., Eckelman W.C., Menkens A.E.
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<em>Essential parameters to consider for the characterization of optical imaging probes.</em>
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<span><span class="ref-journal">Nanomedicine (Lond). </span>2012;<span class="ref-vol">7</span>(7):1101–7.</span> [<a href="/pmc/articles/PMC3445333/" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pmc">PMC free article<span class="bk_prnt">: PMC3445333</span></a>] [<a href="https://pubmed.ncbi.nlm.nih.gov/22846094" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 22846094</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>5.</dt><dd><div class="bk_ref" id="FTP11-Cy7.REF.5">Tung C.H.
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<em>Fluorescent peptide probes for in vivo diagnostic imaging.</em>
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<span><span class="ref-journal">Biopolymers. </span>2004;<span class="ref-vol">76</span>(5):391–403.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/15389488" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 15389488</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>6.</dt><dd><div class="bk_ref" id="FTP11-Cy7.REF.6">Bosman F.T., Stamenkovic I.
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<em>Functional structure and composition of the extracellular matrix.</em>
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<span><span class="ref-journal">J Pathol. </span>2003;<span class="ref-vol">200</span>(4):423–8.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/12845610" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 12845610</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>7.</dt><dd><div class="bk_ref" id="FTP11-Cy7.REF.7">Jiang W.G., Puntis M.C., Hallett M.B.
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<em>Molecular and cellular basis of cancer invasion and metastasis: implications for treatment.</em>
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<span><span class="ref-journal">Br J Surg. </span>1994;<span class="ref-vol">81</span>(11):1576–90.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/7827878" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 7827878</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>8.</dt><dd><div class="bk_ref" id="FTP11-Cy7.REF.8">Pilch J., Brown D.M., Komatsu M., Jarvinen T.A., Yang M., Peters D., Hoffman R.M., Ruoslahti E.
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<em>Peptides selected for binding to clotted plasma accumulate in tumor stroma and wounds.</em>
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<span><span class="ref-journal">Proc Natl Acad Sci U S A. </span>2006;<span class="ref-vol">103</span>(8):2800–4.</span> [<a href="/pmc/articles/PMC1413849/" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pmc">PMC free article<span class="bk_prnt">: PMC1413849</span></a>] [<a href="https://pubmed.ncbi.nlm.nih.gov/16476999" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 16476999</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>9.</dt><dd><div class="bk_ref" id="FTP11-Cy7.REF.9">Corti R., Fuster V.
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<em>New understanding, diagnosis, and prognosis of atherothrombosis and the role of imaging.</em>
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<span><span class="ref-journal">Am J Cardiol. </span>2003;<span class="ref-vol">91</span>(3A):17A–26A.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/12645640" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 12645640</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>10.</dt><dd><div class="bk_ref" id="FTP11-Cy7.REF.10">Lee K.N., Lee C.S., Tae W.C., Jackson K.W., Christiansen V.J., McKee P.A.
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<em>Crosslinking of alpha 2-antiplasmin to fibrin.</em>
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<span><span class="ref-journal">Ann N Y Acad Sci. </span>2001;<span class="ref-vol">936</span>:335–9.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/11460490" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 11460490</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>11.</dt><dd><div class="bk_ref" id="FTP11-Cy7.REF.11">Hara T., Bhayana B., Thompson B., Kessinger C.W., Khatri A., McCarthy J.R., Weissleder R., Lin C.P., Tearney G.J., Jaffer F.A.
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<em>Molecular imaging of fibrin deposition in deep vein thrombosis using fibrin-targeted near-infrared fluorescence.</em>
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<span><span class="ref-journal">JACC Cardiovasc Imaging. </span>2012;<span class="ref-vol">5</span>(6):607–15.</span> [<a href="/pmc/articles/PMC3376390/" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pmc">PMC free article<span class="bk_prnt">: PMC3376390</span></a>] [<a href="https://pubmed.ncbi.nlm.nih.gov/22698530" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 22698530</span></a>]</div></dd></dl></dl></div><div id="bk_toc_contnr"></div></div></div><div class="fm-sec"><h2 id="_NBK138567_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 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 class="small">Corresponding author.</div></div><h3>Publication History</h3><p class="small">Created: <span itemprop="datePublished">April 27, 2013</span>; Last Update: <span itemprop="dateModified">May 30, 2013</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. Cy7-Tyr-d-Glu-Cys-Hyp-Tyr(3-Cl)-Gly-Leu-Cys-Tyr-Ile-Gln-NH2. 2013 Apr 27 [Updated 2013 May 30]. 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/Cy7TetramericRGD/?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/soscypate/?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="figobFTP11Cy7Tncchemicalnamecy7tyrdglucy"><div id="FTP11-Cy7.T.nc_chemical_namecy7tyrdglucy" class="table"><p class="large-table-link" style="display:none"><span class="right"><a href="/books/NBK138567/table/FTP11-Cy7.T.nc_chemical_namecy7tyrdglucy/?report=objectonly" target="object">View in own window</a></span></p><div class="large_tbl" id="__FTP11-Cy7.T.nc_chemical_namecy7tyrdglucy_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;">Cy7-Tyr-<span class="small-caps">d</span>-Glu-Cys-Hyp-Tyr(3-Cl)-Gly-Leu-Cys-Tyr-Ile-Gln-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;">Cy7-FTP11</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;"></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;">Fibrin</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;">Acceptor</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;">Near-infrared (NIR) fluorescence imaging, optical</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;">Cy7</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;">No structure is 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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