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<script type="text/javascript" src="/corehtml/pmc/jatsreader/ptpmc_3.22/js/jr.boots.min.js"> </script><title>Fluorescein-conjugated cyclic decapeptides, CGLIIQKNEC (CLT1) and CNAGESSKNC (CLT2) - Molecular Imaging and Contrast Agent Database (MICAD) - NCBI Bookshelf</title>
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<meta name="citation_date" content="2012/08/28">
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<meta name="citation_author" content="Liang Shan">
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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="_NBK61996_"><span class="title" itemprop="name">Fluorescein-conjugated cyclic decapeptides, CGLIIQKNEC (CLT1) and CNAGESSKNC (CLT2)</span></h1><div itemprop="alternativeHeadline" class="subtitle whole_rhythm">Fluorescent CLT peptides</div><p class="contribs">Shan L.</p><p class="fm-aai"><a href="#_NBK61996_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="figFluorescinCLTTncchemicalnamefluores"><a href="/books/NBK61996/table/Fluorescin-CLT.T.nc_chemical_namefluores/?report=objectonly" target="object" title="Table" class="img_link icnblk_img" rid-ob="figobFluorescinCLTTncchemicalnamefluores"><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="Fluorescin-CLT.T.nc_chemical_namefluores"><a href="/books/NBK61996/table/Fluorescin-CLT.T.nc_chemical_namefluores/?report=objectonly" target="object" rid-ob="figobFluorescinCLTTncchemicalnamefluores">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="Fluorescin-CLT.Background"><h2 id="_Fluorescin-CLT_Background_">Background</h2><p>[<a href="/pubmed?term=tumor%20stroma%20and%20clotted%20plasma" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>Fluorescein-conjugated cyclic decapeptides, CGLIIQKNEC (CLT1) and CNAGESSKNC (CLT2), abbreviated as fluorescent CLT peptides, are two peptide agents that specifically home to tumors and wounds and are potentially useful for tumor-targeted imaging and therapy (<a class="bibr" href="#Fluorescin-CLT.REF.1" rid="Fluorescin-CLT.REF.1">1</a>).</p><p>Tumor tissue is different from normal tissue in the content and function of its stroma. At the initial stage of tumor development, tumor cells secrete growth factors, including vascular permeability factor that renders the local microvasculature hyperpermeable to fibrinogen and other plasma proteins. Extravasated fibrinogen crosslinks with fibrin and other proteins, forming a meshwork in the tumor stroma (<a class="bibr" href="#Fluorescin-CLT.REF.1" rid="Fluorescin-CLT.REF.1 Fluorescin-CLT.REF.2">1, 2</a>). This sequence also occurs in the process of wound-healing and in the progression of many other diseases, but the tumor stroma contains increased amounts of fibrinogen, collagen, fibronectin, fibrinogen-derived products, and other proteins (<a class="bibr" href="#Fluorescin-CLT.REF.3" rid="Fluorescin-CLT.REF.3">3</a>). These proteins either come from the leaky blood vessels or are inappropriately synthesized by the tumor cells. Functionally, normal stroma generates an antiproliferative environment, whereas tumor stroma promotes tumor cell proliferation, migration, and lymphovascular invasion by providing adhesion proteins, proteases, and growth factors (<a class="bibr" href="#Fluorescin-CLT.REF.2" rid="Fluorescin-CLT.REF.2 Fluorescin-CLT.REF.4">2, 4</a>).</p><p>Abnormal formation of clotted plasma protein meshwork in the tumor stroma and on the tumor blood vessel walls has prompted investigators to generate tumor stroma-targeted imaging and therapeutic agents. Pilch et al. screened a phage library on plasma clots and obtained two cyclic decapeptides (CLT; CLT1 and CLT2) (<a class="bibr" href="#Fluorescin-CLT.REF.1" rid="Fluorescin-CLT.REF.1">1</a>). The fluorescence-labeled CLT peptides specifically accumulated in the fibrillar meshwork that existed in the tumor stroma, but they were not detectable in other tissues in animal models of human tumors. Ye et al. conjugated the CLT1 peptide with gadolinium-diethylenetriamine pentaacetic acid (Gd-DTPA), and the generated agent <a href="/books/NBK23114/#Gd-DTPA-CLT1.Background" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">Gd-DTPA-CLT1</a> exhibited high specificity to the fibronectin-fibrin complexes in the tumor stroma (<a class="bibr" href="#Fluorescin-CLT.REF.5" rid="Fluorescin-CLT.REF.5">5</a>). Simberg et al. also reported the clotted plasma protein-targeted multimodal agent <a href="/books/NBK23725/#CREKA-SPIO.Background" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">CREKA-SPIO-Cy7</a>, which was synthesized by conjugation of the peptide CREKA with superparamagnetic iron oxide and cyanine 7 (<a class="bibr" href="#Fluorescin-CLT.REF.6" rid="Fluorescin-CLT.REF.6">6</a>). On the basis of the interaction between the fibrinogen-derived products and heparin, Yuk et al. synthesized the MRI contrast agent, Composite NPs, using heparin as the specific ligand (<a class="bibr" href="#Fluorescin-CLT.REF.7" rid="Fluorescin-CLT.REF.7 Fluorescin-CLT.REF.8">7, 8</a>). Composite NPs have been shown to selectively distribute in tumors in an animal model of murine squamous cell carcinoma (<a class="bibr" href="#Fluorescin-CLT.REF.7" rid="Fluorescin-CLT.REF.7">7</a>). This chapter summarizes the data obtained with the fluorescent CLT peptides (<a class="bibr" href="#Fluorescin-CLT.REF.1" rid="Fluorescin-CLT.REF.1">1</a>).</p><div id="Fluorescin-CLT.Related_Resource_Links"><h3>Related Resource Links:</h3><p>
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<a href="/books/?term=tumor%20stroma%20and%20clotted%20AND%20micad%5bbook%5d" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">Tumor stroma clotted plasma protein-targ</a>
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<a href="/books/?term=tumor%20stroma%20and%20clotted%20AND%20micad%5bbook%5d" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">e</a>
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<a href="/books/?term=tumor%20stroma%20and%20clotted%20AND%20micad%5bbook%5d" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">ted imaging agents in MICAD</a>
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</p></div></div><div id="Fluorescin-CLT.Synthesis"><h2 id="_Fluorescin-CLT_Synthesis_">Synthesis</h2><p>[<a href="/pubmed/?term=16476999" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>CLT1 and CLT2 peptides were identified through screening of a phage library on clotted plasma (<a class="bibr" href="#Fluorescin-CLT.REF.1" rid="Fluorescin-CLT.REF.1">1</a>). The phage selection was designed to amplify phages that bind to plasma clots but not to anticoagulated plasma. Three rounds of selection produced a pool of phages with seven-fold increased binding to plasma clots. Additional selection rounds did not increase the binding. Sequencing showed that the phages encoding the peptide inserts CLT1 and CLT2 were highly enriched among the clot-binding phages.</p><p>Peptides were then synthesized, conjugated to fluorescein isothiocyanate, and cyclized by exposure to air. A control peptide with the sequence of KAREC was also synthesized and labeled with fluorescein. The efficiency of fluorescein labeling was not reported.</p></div><div id="Fluorescin-CLT.In_Vitro_Studies_Testing"><h2 id="_Fluorescin-CLT_In_Vitro_Studies_Testing_">In Vitro Studies: Testing in Cells and Tissues</h2><p>[<a href="/pubmed/?term=16476999" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>The CLT peptides, CLT1 and CLT2, exhibited three- to four-fold increased efficiency of binding to plasma clots compared to the control peptide. They did not significantly bind to clots made of purified fibrin or fibronectin immobilized on plastic (results not shown). These results indicate that the two peptides specifically bind to clots containing fibrin and fibronectin (<a class="bibr" href="#Fluorescin-CLT.REF.1" rid="Fluorescin-CLT.REF.1">1</a>).</p></div><div id="Fluorescin-CLT.Animal_Studies"><h2 id="_Fluorescin-CLT_Animal_Studies_">Animal Studies</h2><div id="Fluorescin-CLT.Rodents"><h3>Rodents</h3><p>[<a href="/pubmed/?term=16476999" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>Pilch et al. tested the homing of CLT1 and CLT2 in tumors produced in BALB/c nu/nu mice, mouse mammary tumor virus (MMTV) PyMT mice, fibrinogen knockout mice, and transgenic plasma fibronectin-deficient C57BL/6-Fn(fl/fl)<i>Mx-Cre</i><sup>+</sup> mice and their wild-type littermates (<a class="bibr" href="#Fluorescin-CLT.REF.1" rid="Fluorescin-CLT.REF.1">1</a>). The MMTV-PyMT mice develop breast cancer under the influence of a polyoma middle T antigen driven by the mouse tumor virus promoter. Imaging of the whole tissues ex vivo was performed with a Leica fluorescence stereomicroscope at 3 h after the peptide injection.</p><p>BALB/c nu/nu mice bearing orthotopic MDA-MB-435 xenograft tumors (human breast cancer) were intravenously injected with fluorescent CLT1 (<i>n</i> = 6), CLT2 (<i>n</i> = 4), or the control peptide (<i>n</i> = 4). Intense fluorescence was observed in the tumors from the mice injected with CLT1 and CLT2, but not in the tumors from the mice injected with the control peptide. No fluorescence was observed in healthy organs of the CLT-injected animals. Microscopy showed that the fluorescence from the CLT peptides and the fluorescence from the fibrin staining colocalized in tumor sections. CLT peptides also co-distributed with fibronectin (data not shown). The co-distribution results of the CLT peptides, fibrin, and fibronectin in the MMTV-PyMT transgenic breast tumors were identical to those obtained with the MDA-MB-435 xenografts (data not shown). These results suggest that CLT peptides are associated with the fibrin and fibronectin in tumor stroma.</p><p>Fibrinogen knockout mice bearing B16-F1 tumors (mouse melanoma) were used to study the role of fibrin, fibrinogen, and fibronectin in the homing of the CLT peptides to tumors. The CLT peptides homed to B16-F1 tumors grown in the wild-type C57BL/6 mice (<i>n</i> = 10), which produce a fibrillar meshwork. In contrast, only faint, evenly distributed fluorescence was observed in tumors (<i>n</i> = 4) grown in the fibrinogen knockout mice, which lack the ability to produce fibrin. In plasma fibronectin-deficient mice, B16-F1 tumors grown in wild-type littermates also accumulated CLT peptides in the fibrillar matrix, but mice lacking plasma fibronectin did not (<i>n</i> = 6 mice). Unlike in the model of fibrinogen knockout mice, there was no residual peptide binding to the tumors in the model of plasma fibronectin-deficient mice. These results suggest that both fibrin and fibronectin from plasma are needed for the homing of CLT peptides in tumors.</p><p>CLT peptide homing to injured tissue was tested in mice with wire injury of the femoral artery and in mice with skin incisions (<a class="bibr" href="#Fluorescin-CLT.REF.1" rid="Fluorescin-CLT.REF.1">1</a>). Fluorescent CLT peptides homed to the de-endothelialized femoral arteries (<i>n</i> = 5), producing strong fluorescence in the vessel wall. CLT homing was also seen in crush injuries of the muscle (<i>n</i> = 3) and in skin wounds resulting from incisions (<i>n</i> = 4). No CLT peptide homing was observed in intact arteries, muscles, skin, or other healthy tissues of the mice with injuries. The control peptide showed no homing to the injured tissues (data not shown) suggesting the specificity of CLT peptides.</p></div><div id="Fluorescin-CLT.Other_NonPrimate_Mammals"><h3>Other Non-Primate Mammals</h3><p>[<a href="/pubmed/?term=%22SUBSTANCENAME%22%5BSubstance%20Name%5D%20AND%20%28dog%20OR%20rabbit%20OR%20pig%20OR%20sheep%29" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>No references are available.</p></div><div id="Fluorescin-CLT.NonHuman_Primates"><h3>Non-Human Primates</h3><p>[<a href="/pubmed/?term=%22SUBSTANCENAME%22%5BSubstance%20Name%5D%20AND%20%28primate%20NOT%20human%29" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>No references are available.</p></div></div><div id="Fluorescin-CLT.Human_Studies"><h2 id="_Fluorescin-CLT_Human_Studies_">Human Studies</h2><p>[<a href="/pubmed/?term=%22SUBSTANCENAME%22%5BSubstance%20Name%5D%20AND%20human" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>No references are available.</p></div><div id="Fluorescin-CLT.References"><h2 id="_Fluorescin-CLT_References_">References</h2><dl class="temp-labeled-list"><dl class="bkr_refwrap"><dt>1.</dt><dd><div class="bk_ref" id="Fluorescin-CLT.REF.1">Pilch J., Brown D.M., Komatsu M., Jarvinen T.A., Yang M., Peters D., Hoffman R.M., Ruoslahti E. Peptides selected for binding to clotted plasma accumulate in tumor stroma and wounds. <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>2.</dt><dd><div class="bk_ref" id="Fluorescin-CLT.REF.2">Simpson-Haidaris P.J., Rybarczyk B. Tumors and fibrinogen. The role of fibrinogen as an extracellular matrix protein. <span><span class="ref-journal">Ann N Y Acad Sci. </span>2001;<span class="ref-vol">936</span>:406–25.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/11460495" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 11460495</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>3.</dt><dd><div class="bk_ref" id="Fluorescin-CLT.REF.3">Rybarczyk B.J., Lawrence S.O., Simpson-Haidaris P.J. Matrix-fibrinogen enhances wound closure by increasing both cell proliferation and migration. <span><span class="ref-journal">Blood. </span>2003;<span class="ref-vol">102</span>(12):4035–43.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/12920033" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 12920033</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>4.</dt><dd><div class="bk_ref" id="Fluorescin-CLT.REF.4">Malik G., Knowles L.M., Dhir R., Xu S., Yang S., Ruoslahti E., Pilch J. Plasma fibronectin promotes lung metastasis by contributions to fibrin clots and tumor cell invasion. <span><span class="ref-journal">Cancer Res. </span>2010;<span class="ref-vol">70</span>(11):4327–34.</span> [<a href="/pmc/articles/PMC2880218/" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pmc">PMC free article<span class="bk_prnt">: PMC2880218</span></a>] [<a href="https://pubmed.ncbi.nlm.nih.gov/20501851" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 20501851</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>5.</dt><dd><div class="bk_ref" id="Fluorescin-CLT.REF.5">Ye F., Wu X., Jeong E.K., Jia Z., Yang T., Parker D., Lu Z.R. A peptide targeted contrast agent specific to fibrin-fibronectin complexes for cancer molecular imaging with MRI. <span><span class="ref-journal">Bioconjug Chem. </span>2008;<span class="ref-vol">19</span>(12):2300–3.</span> [<a href="/pmc/articles/PMC2651601/" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pmc">PMC free article<span class="bk_prnt">: PMC2651601</span></a>] [<a href="https://pubmed.ncbi.nlm.nih.gov/19053180" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 19053180</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>6.</dt><dd><div class="bk_ref" id="Fluorescin-CLT.REF.6">Simberg D., Duza T., Park J.H., Essler M., Pilch J., Zhang L., Derfus A.M., Yang M., Hoffman R.M., Bhatia S., Sailor M.J., Ruoslahti E. Biomimetic amplification of nanoparticle homing to tumors. <span><span class="ref-journal">Proc Natl Acad Sci U S A. </span>2007;<span class="ref-vol">104</span>(3):932–6.</span> [<a href="/pmc/articles/PMC1783417/" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pmc">PMC free article<span class="bk_prnt">: PMC1783417</span></a>] [<a href="https://pubmed.ncbi.nlm.nih.gov/17215365" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 17215365</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>7.</dt><dd><div class="bk_ref" id="Fluorescin-CLT.REF.7">Yuk S.H., Oh K.S., Cho S.H., Lee B.S., Kim S.Y., Kwak B.K., Kim K., Kwon I.C. Glycol chitosan/heparin immobilized iron oxide nanoparticles with a tumor-targeting characteristic for magnetic resonance imaging. <span><span class="ref-journal">Biomacromolecules. </span>2011;<span class="ref-vol">12</span>(6):2335–43.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/21506550" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 21506550</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>8.</dt><dd><div class="bk_ref" id="Fluorescin-CLT.REF.8">Norrby K. Low-molecular-weight heparins and angiogenesis. <span><span class="ref-journal">APMIS. </span>2006;<span class="ref-vol">114</span>(2):79–102.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/16519745" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 16519745</span></a>]</div></dd></dl></dl></div><div id="bk_toc_contnr"></div></div></div><div class="fm-sec"><h2 id="_NBK61996_pubdet_">Publication Details</h2><h3>Author Information and Affiliations</h3><div class="contrib half_rhythm"><span itemprop="author">Liang Shan</span>, PhD<div class="affiliation small">National Center for Biotechnology Information, NLM, NIH<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">July 28, 2011</span>; Last Revision: <span itemprop="dateModified">August 28, 2012</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>Shan L. Fluorescein-conjugated cyclic decapeptides, CGLIIQKNEC (CLT1) and CNAGESSKNC (CLT2) 2011 Jul 28 [Updated 2012 Aug 28]. 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/FITC-IAC/?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/sosgreenfluorescencepro/?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="figobFluorescinCLTTncchemicalnamefluores"><div id="Fluorescin-CLT.T.nc_chemical_namefluores" class="table"><p class="large-table-link" style="display:none"><span class="right"><a href="/books/NBK61996/table/Fluorescin-CLT.T.nc_chemical_namefluores/?report=objectonly" target="object">View in own window</a></span></p><div class="large_tbl" id="__Fluorescin-CLT.T.nc_chemical_namefluores_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;">Fluorescein-conjugated cyclic decapeptides, CGLIIQKNEC (CLT1) and CNAGESSKNC (CLT2)</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;">Fluorescent CLT peptides</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;">Fluorescent CLT1, fluorescent CLT2</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;">Peptides</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;">Clotted plasma proteins (fibrin and fibronectin)</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;">Others (proteins)</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;">Optical imaging</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;">Fluorescein</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.</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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