<result><BiopanningDataSet><Item><BiopanningDataSetID>2476</BiopanningDataSetID>
<Peptides>RGLFTEWFRGGSWSNYRVTS</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:11602024</Reference>
<Target_Name>MRNA of amyloid precursor protein (APP)</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>X20 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>For the mRNA pans, all solutions and surfaces are pretreated with DEPC or RNaseZap, respectively, to eliminate RNase contamination that may compromise the integrity of the RNA. The biotinylated RNA solution was added to an appropriate number of wells in a 96-well microtiter plate precoated with Streptavidin (Pierce).</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2477</BiopanningDataSetID>
<Peptides>TDGGRSVISDNVRGGSRLWLWIRHGSWSQAWGPQDAWSSK
RVSSAQPGCTSRVRFRCPRGGLLFNGVTSTNPKTGLSNAQ</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:11602024</Reference>
<Target_Name>MRNA of amyloid precursor protein (APP)</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>X40 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>For the mRNA pans, all solutions and surfaces are pretreated with DEPC or RNaseZap, respectively, to eliminate RNase contamination that may compromise the integrity of the RNA. The biotinylated RNA solution was added to an appropriate number of wells in a 96-well microtiter plate precoated with Streptavidin (Pierce).</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2478</BiopanningDataSetID>
<Peptides>WPPGRTLSDLIRGGAGARGM
SSGGLHRWSALRGGHGHGLA</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:11602024</Reference>
<Target_Name>MRNA of hepatitis C virus (HCV)</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>X20 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>For the mRNA pans, all solutions and surfaces are pretreated with DEPC or RNaseZap, respectively, to eliminate RNase contamination that may compromise the integrity of the RNA. The biotinylated RNA solution was added to an appropriate number of wells in a 96-well microtiter plate precoated with Streptavidin (Pierce).</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2479</BiopanningDataSetID>
<Peptides>AMRLKPIAFKGPRAGAGWVEVQPCFAAFRAACTRGGSHHH
LHAGWDVTAPRRACKGAQGPGLHGRFYCHRGGLCSGLGRC
DEQSSLKGKLRGALVRLGMGHAMPHRGGVWPSTGRPSKQG
WTPRHGPMRCWRHQSVFPVGAGPHWALWPIKGPRGGRTAC
PKTGSNIWLPLYHKVCPASTRAGNGRGGSRFLWGSMQTNC</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>5</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:11602024</Reference>
<Target_Name>MRNA of hepatitis C virus (HCV)</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>X40 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>For the mRNA pans, all solutions and surfaces are pretreated with DEPC or RNaseZap, respectively, to eliminate RNase contamination that may compromise the integrity of the RNA. The biotinylated RNA solution was added to an appropriate number of wells in a 96-well microtiter plate precoated with Streptavidin (Pierce).</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2480</BiopanningDataSetID>
<Peptides>RLQRRGGGAVAVVWVGFGVGLLWGRLLLIILGWVLMWFLS
QHSEHGGTEWRKRGGMAFAASFLCMRDSYRTTRLRSLLG
GTRHVINRVRDSSGVPCKRFGGLQFSQMGKCTIPRGGA</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>3</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:11602024</Reference>
<Target_Name>MRNA of insulin-like growth factor-1 (IGF-1)</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>X40 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>For the mRNA pans, all solutions and surfaces are pretreated with DEPC or RNaseZap, respectively, to eliminate RNase contamination that may compromise the integrity of the RNA. The biotinylated RNA solution was added to an appropriate number of wells in a 96-well microtiter plate precoated with Streptavidin (Pierce).</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2481</BiopanningDataSetID>
<Peptides>VLRGGSVGKGSLMWCQEVDWRTGGPRSNLWGLWNGRQPPK</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:11602024</Reference>
<Target_Name>MRNA of Rev Response Element (RRE)</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>X40 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>For the mRNA pans, all solutions and surfaces are pretreated with DEPC or RNaseZap, respectively, to eliminate RNase contamination that may compromise the integrity of the RNA. The biotinylated RNA solution was added to an appropriate number of wells in a 96-well microtiter plate precoated with Streptavidin (Pierce).</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2482</BiopanningDataSetID>
<Peptides>VVYVGVLSYWPHLSGGGRLQVRCLIGRGGFGCRGG</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:11602024</Reference>
<Target_Name>MRNA of amyloid precursor protein (APP)</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>X40 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>For the mRNA pans, all solutions and surfaces are pretreated with DEPC or RNaseZap, respectively, to eliminate RNase contamination that may compromise the integrity of the RNA. The biotinylated RNA solution was added to an appropriate number of wells in a 96-well microtiter plate precoated with Streptavidin (Pierce).</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2483</BiopanningDataSetID>
<Peptides>CRGRRST
CRSRKG
CKAAKNK
CKGAKAR
FRVGVADV</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>5</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>2</Rounds_of_Panning>
<Reference>PMID:14667506</Reference>
<Target_Name>RIP1-Tag2 tumors</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-C7C phage display library (CX7C)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>The screening process involved two ex vivo selection rounds followed by 2 in vivo selection rounds.</Brief_Description>
<BiopanningDataSet_Comments>Fluorescence detection assay showed that no peptides homed appreciably to normal pancreatic islets or other organs. Besides, The relative homing efficiencies in the various tumor models of the phage from the RIP1-Tag2 tumor screen fall broadly into two categories: those that selectively home to RIP1-Tag2 tumors (CKAAKNK, CRGRRST, FRVGVADV) and those that show a more general homing to other tumors in addition to RIP1-Tag2 (VGVG, CKGAKAR). The phage homing data were supported by i.v. injection of fluorescein-conjugated peptides corresponding to the phage. Peptide CRGRRST is homologous with pro-PDGF-B, which is expressed in endothelial cells, while its receptor is expressed in pericytes.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2484</BiopanningDataSetID>
<Peptides>CEYQLDVE</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:14667506</Reference>
<Target_Name>RIP1-Tag2 angiogenic islets</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-C7C phage display library (CX7C)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>The screening process involved two ex vivo selection rounds followed by 3 in vivo selection rounds.</Brief_Description>
<BiopanningDataSet_Comments>Fluorescence detection assay showed that the peptide CEYQLDVE didn't home appreciably to normal pancreatic islets or other organs.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2485</BiopanningDataSetID>
<Peptides>CWDDGWLC(131)
CWDDLWWLC(10)
CWDDGLMC(7)
CWDDGWMC(4)</Peptides>
<Motif>CWDD[GL]WLC</Motif>
<Unique_Sequence_Number>4</Unique_Sequence_Number>
<Experimental_Method>Phage display (competitive panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:7657703</Reference>
<Target_Name>Fibronectin type Ⅲ10(RGD)-containing fragments</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>CX5C+CX6C+CX7C+CX9 phage display library pool</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>After the fourth panning, wells with bound phages were eluted with 1 mM solution of GRGDSP or *CELRGDGWC* peptidee.</Brief_Description>
<BiopanningDataSet_Comments>A predominant cyclic motif, *CWDD[GL]WLC*, was obtained (the asterisks denote a potential disulfide bond). Studies using the purified phage and the corresponding synthetic cyclic peptides showed that *CWDDGWLC*-expressing phage binds specifically to fibronectin and to fibronectin fragments containing the RGD sequence. The binding did not require divalent cations and was inhibited by both RGD and *CWDDGWLC*-containing synthetic peptides. Conversely, RGD-expressing phage attached specifically to immobilized *CWDDGWLC*-peptide and the binding could be blocked by the respective synthetic peptides in solution. Moreover, fibronectin bound to a *CWDDGWLC*-peptide affinity column, and could be eluted with an RGD-containing peptide. The *CWDDGWLC*-peptide inhibited RGD-dependent cell attachment to fibronectin and vitronectin, but not to collagen.A region of the β3 subunit of RGD-binding integrins that has been previously demonstrated to be involved in ligand binding includes a polypeptide stretch, KDDLW (in β3) similar to WDDC/LWL. Synthetic peptides corresponding to this region in β3 were found to bind RGD-displaying phage and conversion of its two aspartic residues into alanines greatly reduced the RGD binding. Polyclonal antibodies raised against the *CWDDGWLC*-peptide recognized β1 and β3 in immunoblots. These data indicate that the *CWDDGWLC*-peptide is a functional mimic of ligand binding sites of RGD-directed integrins, and that the structurally similar site in the integrin β subunit is a binding site for RGD.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2486</BiopanningDataSetID>
<Peptides>CWDDGWLC(21)
CLVWLLVQFY(2)
CTFGGGIGRV(l)
CTLRFQRSC(1)</Peptides>
<Motif>CWDD[GL]WLC</Motif>
<Unique_Sequence_Number>4</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:7657703</Reference>
<Target_Name>Fibronectin type Ⅲ10(RGD)-containing fragments</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>CX5C+CX6C+CX7C+CX9 phage display library pool</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>After the fourth panning, wells with bound phages were eluted with 2 mM EDTA.</Brief_Description>
<BiopanningDataSet_Comments>A predominant cyclic motif, *CWDD[GL]WLC*, was obtained (the asterisks denote a potential disulfide bond). Studies using the purified phage and the corresponding synthetic cyclic peptides showed that *CWDDGWLC*-expressing phage binds specifically to fibronectin and to fibronectin fragments containing the RGD sequence. The binding did not require divalent cations and was inhibited by both RGD and *CWDDGWLC*-containing synthetic peptides. Conversely, RGD-expressing phage attached specifically to immobilized *CWDDGWLC*-peptide and the binding could be blocked by the respective synthetic peptides in solution. Moreover, fibronectin bound to a *CWDDGWLC*-peptide affinity column, and could be eluted with an RGD-containing peptide. The *CWDDGWLC*-peptide inhibited RGD-dependent cell attachment to fibronectin and vitronectin, but not to collagen.A region of the β3 subunit of RGD-binding integrins that has been previously demonstrated to be involved in ligand binding includes a polypeptide stretch, KDDLW (in β3) similar to WDDC/LWL. Synthetic peptides corresponding to this region in β3 were found to bind RGD-displaying phage and conversion of its two aspartic residues into alanines greatly reduced the RGD binding. Polyclonal antibodies raised against the *CWDDGWLC*-peptide recognized β1 and β3 in immunoblots. These data indicate that the *CWDDGWLC*-peptide is a functional mimic of ligand binding sites of RGD-directed integrins, and that the structurally similar site in the integrin β subunit is a binding site for RGD.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2487</BiopanningDataSetID>
<Peptides>CWDDGWLC(45)
CSWDDGWLC(6)
CPDDLWWLC(3)
CDGWLGFC(2)
CQRIVLGFT(1)
CDYWLGFC(1)
CFVLWLVC(1)
CGNRLRC(1)</Peptides>
<Motif>CWDD[GL]WLC</Motif>
<Unique_Sequence_Number>8</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:7657703</Reference>
<Target_Name>Fibronectin type Ⅲ10(RGD)-containing fragments</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>CX5C+CX6C+CX7C+CX9 phage display library pool</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>After the fourth panning, wells with bound phages were directly incubated with 50 μl of bacteria.</Brief_Description>
<BiopanningDataSet_Comments>A predominant cyclic motif, *CWDD[GL]WLC*, was obtained (the asterisks denote a potential disulfide bond). Studies using the purified phage and the corresponding synthetic cyclic peptides showed that *CWDDGWLC*-expressing phage binds specifically to fibronectin and to fibronectin fragments containing the RGD sequence. The binding did not require divalent cations and was inhibited by both RGD and *CWDDGWLC*-containing synthetic peptides. Conversely, RGD-expressing phage attached specifically to immobilized *CWDDGWLC*-peptide and the binding could be blocked by the respective synthetic peptides in solution. Moreover, fibronectin bound to a *CWDDGWLC*-peptide affinity column, and could be eluted with an RGD-containing peptide. The *CWDDGWLC*-peptide inhibited RGD-dependent cell attachment to fibronectin and vitronectin, but not to collagen.A region of the β3 subunit of RGD-binding integrins that has been previously demonstrated to be involved in ligand binding includes a polypeptide stretch, KDDLW (in β3) similar to WDDC/LWL. Synthetic peptides corresponding to this region in β3 were found to bind RGD-displaying phage and conversion of its two aspartic residues into alanines greatly reduced the RGD binding. Polyclonal antibodies raised against the *CWDDGWLC*-peptide recognized β1 and β3 in immunoblots. These data indicate that the *CWDDGWLC*-peptide is a functional mimic of ligand binding sites of RGD-directed integrins, and that the structurally similar site in the integrin β subunit is a binding site for RGD.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2488</BiopanningDataSetID>
<Peptides>SVSVGMKPSPRP(3)
ASPMPTAKLRFA(1)
NWTTNRPNNTSP(1)
MNNDHVPSVAQG(1)
AYWSNPESHPXQ(1)
SNPFSKPYGLTV(1)
WDSNTYTPRPLM(1)
ATNPTHPGHLPV(1)
NPSLHKPLTISI(1)
NPYQHRNWAYVG(1)
HARENSLPWLHA(1)
YPHYSLPGSSTL(1)
LPLALPRHNASV(1)
SSLKLHQTPLDA(1)
SSLEPWHRTTSR(1)
GSIALSSWLSLP(1)
GNFQSESYFVPH(1)
GLHESTFTQRRL(1)
FSHELSWKPRKA(1)
NYLHNHPYGTVG(1)
LNYFTLSSKRE(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>21</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:19276080</Reference>
<Target_Name>SAS-derived tumors</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>SAS cells were injected subcutaneously into the dorsolateral flank of 4–6-week-old SCID mice to produce oral cancer xenografts. The phage-displayed peptide library was injected intravenously into the tail vein of SCID mice bearing size-matched SAS-derived tumors.</Brief_Description>
<BiopanningDataSet_Comments>From 30 random selected phage clones, 23 phage-displayed peptide sequences were identified. Six novel peptides (NYLHNHPYGTVG, SNPFSKPYGLTV, GLHESTFTQRRL, YPHYSLPGSSTL, SSLEPWHRTTSR and LPLALPRHNASV) were identified as being able to recognize tumor vasculature but not normal blood vessels in severe combined immunodeficiency (SCID) mice bearing human tumors. These tumor-homing peptides also bound to blood vessels in surgical specimens of various human cancers. The peptidelinked liposomes containing fluorescent substance were capable of translocating across the plasma membrane through endocytosis. With the conjugation of peptides and liposomal doxorubicin, the targeted drug delivery systems enhanced the therapeutic efficacy of the chemotherapeutic agent against human cancer xenografts by decreasing tumor angiogenesis and increasing cancer cell apoptosis. Furthermore, the peptide-mediated targeting liposomes improved the pharmacokinetics and pharmacodynamics of the drug they delivered compared with nontargeting liposomes or free drugs. It indicates that the tumor-homing peptides can be used specifically target tumor vasculature and have the potential to improve the systemic treatment of patients with solid tumors.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2489</BiopanningDataSetID>
<Peptides>IVWHRWYAWSPASRI[581.1 ± 98.0]
YYAWHWYAWSPKSV[69.9 ± 19.6]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:12760424</Reference>
<Target_Name>Thomsen-Friedenreich antigen (T antigen, TF antigen)</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>fUSE5 X5WYA[WF]SPX4 phage dsiplay library</Library_Name>
<Affinity_Measurement_Method>Fluorescence</Affinity_Measurement_Method>
<Affinity_Measurement_Description>Binding of the peptides to the TF antigen displayed on ASF was detected by observing a quenching of AlexaFluor 488 fluorescence. The dissociation constant (Kd, nM) that described binding affinity was calculated. The value of the first-generation peptide, P30 (HGRFILPWWYAFSPS), was 321.9 ± 70.0. And the control peptide, RNVPPIFNDVYWIAF, showed no detectable binding.</Affinity_Measurement_Description>
<Brief_Description>Thomsen-Friedenreich (TF) antigen conjugated to human serum albumin (HSA) was immobilized on a streptavidin-coated Petri dish.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2490</BiopanningDataSetID>
<Peptides>ADITDPMGA(2)
AVSPNVHDG(2)
AAPDLQDAM(1)
ADRLNSDAG(1)
ADRPSTTSL(1)
ADPPRTVST(1)
ADRPSMSPT(1)
ADRTSNAST(1)
ADKSYIPSS(1)
AVRNPSHHS(1)
ADPTPRGHS(1)
ADPTRQPHS(1)
AEHQNSAGP(1)
ADARSAGAIS(1)
ADSKNAGPM(1)
AETKFSGSA(1)
ADPKGSGVT(1)
AGLTSPNDM(1)
AVGTHTPDS(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>19</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning></Rounds_of_Panning>
<Reference>PMID:12089009</Reference>
<Target_Name>Phytophthora capsici zoospore</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>f8-8mer phage display library (X8)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>In the affinity selection procedure, P. capsici zoospores were added to phage in the presence of 50 mM LiCl, which prevents zoospore encystment.</Brief_Description>
<BiopanningDataSet_Comments>The abilities of phage clones to induce encystment varied. For example, at a concentration of 2.5e9 virions/μl, clones Pc78 (displaying ADPPRTVST), Pc87 (displaying ADRPSMSPT), Pc64 (displaying ADITDPMGA), and Pc42 (displaying AVSPNVHDG) induced &gt;80% encystment within 20 min. Conversely, only about 20% of zoospores exposed to Pc56 (displaying AAPDLQDAM), Pc45 (displaying AEHQNSAGP), Pc15B (displaying AGLTSPNDM), or the fuse5 phage vector were encysted during this period. In solution, 200 μM peptide 87, corresponding to phage Pc87, induced complete encystment of zoospores. In contrast, peptide 56, corresponding to the ineffectual phage Pc56, did not induce significant encystment at the same concentration. Peptide 42, corresponding to phage Pc42, induced an intermediate level of encystment.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2491</BiopanningDataSetID>
<Peptides>MTHDPVISLPTT
LHRHSHGHSYKS
GHWHNHRHQAPL
KYPHQHLHMHDS
IGWHYYLRTQHS
YPFHHKHWHRPN
ANIVPIHANHFQ
MHKHPHGSQGPT
YKLPGHHHHYRP</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>9</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning></Rounds_of_Panning>
<Reference>PMID:12795832</Reference>
<Target_Name>CD147</Target_Name>
<Template_Name>Metuximab</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2492</BiopanningDataSetID>
<Peptides>GNVPDMRHIARP[420 ± 30]
LTNGPHIPPDHP[430 ± 50]
DYQHATKTGPHL[NT]
APIMIQCPTPHT[NT]
PYTHAATPPHSP[NT]
SPPDFXMRPPHG[NT]
VPPKPSRPASMW[NT]
XPPYAVLAPTAL[NT]
SAHEPPGSQRVA[NT]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>9</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning, competitive panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:17132933</Reference>
<Target_Name>HIV-1 TAR</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method>Binding assay</Affinity_Measurement_Method>
<Affinity_Measurement_Description>The association of the purified peptides to TAR was determined by filter binding assay. The dissociation constant KD (nM) value was calculated.</Affinity_Measurement_Description>
<Brief_Description>The library  was counter-selected by two successive incubations in the presence of streptavidin coatd beads. Nonbinding phages were recovered and incubated with 3' biotinylated TAR. The mix was then added to streptavidin beads. In the subsequent rounds, competitor yeast tRNA was added. No magnesium was used in the first selection round, but magnesium was used in subsequent selection rounds.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2493</BiopanningDataSetID>
<Peptides>LTNGPHIPPDHP[430 ± 50]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning, competitive panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:17132933</Reference>
<Target_Name>HIV-1 TAR</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method>Binding assay</Affinity_Measurement_Method>
<Affinity_Measurement_Description>The association of the purified peptides to TAR was determined by filter binding assay. The dissociation constant KD (nM) value was calculated.</Affinity_Measurement_Description>
<Brief_Description>The library  was counter-selected by two successive incubations in the presence of streptavidin coatd beads. Nonbinding phages were recovered and incubated with 3' biotinylated TAR. The mix was then added to streptavidin beads. In the subsequent rounds, competitor yeast tRNA was added.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2494</BiopanningDataSetID>
<Peptides>KVSSPPSPPHIL[550 ± 50]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning, competitive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:17132933</Reference>
<Target_Name>HIV-1 TAR</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method>Binding assay</Affinity_Measurement_Method>
<Affinity_Measurement_Description>The association of the purified peptides to TAR was determined by filter binding assay. The dissociation constant KD (nM) value was calculated.</Affinity_Measurement_Description>
<Brief_Description>The library  was counter-selected by two successive incubations in the presence of streptavidin coatd beads. Nonbinding phages were recovered and incubated with 3' biotinylated TAR. The mix was then added to streptavidin beads. In the subsequent rounds, competitor yeast tRNA was added.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2495</BiopanningDataSetID>
<Peptides>GNVPDMRHIARP[420 ± 30]
IXAKDQNTWPRR[NT]
VEWPAQRHHHIP[NT]
YASKFPHLXTLE[NT]
HLSLPQAPTLLP[NT]
ADLPSLFASRGT[NT]</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>6</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning, competitive panning)</Experimental_Method>
<Rounds_of_Panning>2</Rounds_of_Panning>
<Reference>PMID:17132933</Reference>
<Target_Name>HIV-1 TAR</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method>Binding assay</Affinity_Measurement_Method>
<Affinity_Measurement_Description>The association of the purified peptides to TAR was determined by filter binding assay. The dissociation constant KD (nM) value was calculated. NT denotes not tested.</Affinity_Measurement_Description>
<Brief_Description>The library  was counter-selected by two successive incubations in the presence of streptavidin coatd beads. Nonbinding phages were recovered and incubated with 3' biotinylated TAR. The mix was then added to streptavidin beads. In the subsequent rounds, competitor yeast tRNA was added. </Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2496</BiopanningDataSetID>
<Peptides>CGLIIQKNEC(3/24)
CNAGESSKNC(2/24)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (competitive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:16476999</Reference>
<Target_Name>Human plasma clots</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>CX8C T7 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Human plasma clots were incubated with the CX8C peptide library and extensively washed with PBS. Plasma was then added to the clot to remove phage recognizing soluble plasma components.</Brief_Description>
<BiopanningDataSet_Comments>When injected intravenously into mice bearing various types of tumors, fluorescein-conjugated CLT peptides (CGLIIQKNEC and CNAGESSKNC) accumulated in a fibrillar meshwork in the extracellular compartment of the tumors, but were not detectable in other tissues of the tumor-bearing mice. The tumor homing of both peptides was strongly reduced after coinjection with unlabeled CLT2 (CNAGESSKNC), indicating that the two peptides recognize the same binding site. The CLT peptide fluorescence colocalized with staining for fibrin(ogen) present in the extravascular compartment of tumors, but not in other tissues. The CLT peptides did not home to tumors grown in fibrinogen-null mice or in mice that lack plasma fibronectin. The CLT peptides also accumulated at the sites of injury in arteries, skeletal muscle, and skin. It is concluded that the CLT peptides recognize fibrin–fibronectin complexes formed by clotting of plasma proteins that have leaked into the extravascular space in tumors and other lesions. These peptides may be useful in targeting diagnostic and therapeutic materials into tumors and injured tissues.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2497</BiopanningDataSetID>
<Peptides>CHWSFGIFC(8)
CHWMFSPWC(3)
CPWYFLPWC(2)
CPWYFQPWC(2)
CPWYFHPYC(1)
CPWYFFDLC(1)
CPWYFFGAC(1)
CSWIFWEYC(1)
CSWIFWQYC(1)
CSWIFWVYC(1)</Peptides>
<Motif>x-W-x-F-x(3)</Motif>
<Unique_Sequence_Number>10</Unique_Sequence_Number>
<Experimental_Method>Phage display (competitive panning)</Experimental_Method>
<Rounds_of_Panning>3-5</Rounds_of_Panning>
<Reference>PMID:9094664</Reference>
<Target_Name>Puumala virus</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>CX7C phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Biopanning with MAb 4G2 as the eluting antibody included three antibody and two acid elution rounds. In the first panning, the wells were rinsed 10 times with 5% NFDMP-TBS, pre-eluted with antibody 5A2, rinsed three times, and eluted with MAb 4G2. The second panning was done directly with MAb 4G2, whereas in the third, MAb3H9 was used as a pre-eluting MAb. For removal of residual antibody, the phage amplification product of the third panning was treated with Prosep-A (Bioprocessing Ltd.). The fourth panning was done conventionally with 0.1 M HCl-glycine, pH2.2, containing 1mg of BSA per ml as the eluent.</Brief_Description>
<BiopanningDataSet_Comments>The peptide insert, CHWMFSPWC, when displayed on the phages, completely inhibited Puumala virus infection in cell culture at the same effective concentration as the eluting antibody specificfor envelope glycoprotein G2.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2498</BiopanningDataSetID>
<Peptides>CLFNWPVNC(5)
CLFTWPASC(1)
CLFTWPVSC(1)</Peptides>
<Motif>L-F-[NT]-W-P-[VA]-[NS]</Motif>
<Unique_Sequence_Number>3</Unique_Sequence_Number>
<Experimental_Method>Phage display (competitive panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:9094664</Reference>
<Target_Name>Puumala virus</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>CX7C phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Biopanning with MAb 4G2 as the eluting antibody included three antibody and two acid elution rounds. In the first panning, the wells were rinsed 10 times with 5% NFDMP-TBS, pre-eluted with antibody 5A2, rinsed three times, and eluted with MAb 4G2. The second panning was done directly with MAb 4G2, whereas in the third, MAb3H9 was used as a pre-eluting MAb. For removal of residual antibody, the phage amplification product of the third panning was treated with Prosep-A (Bioprocessing Ltd.). The fourth panning was done conventionally with 0.1 M HCl-glycine, pH2.2, containing 1mg of BSA per ml as the eluent.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2499</BiopanningDataSetID>
<Peptides>CPGWWPYPC(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (competitive panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:9094664</Reference>
<Target_Name>Puumala virus</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>CX7C phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Biopanning with MAb 4G2 as the eluting antibody included three antibody and two acid elution rounds. In the first panning, the wells were rinsed 10 times with 5% NFDMP-TBS, pre-eluted with antibody 5A2, rinsed three times, and eluted with MAb 4G2. The second panning was done directly with MAb 4G2, whereas in the third, MAb3H9 was used as a pre-eluting MAb. For removal of residual antibody, the phage amplification product of the third panning was treated with Prosep-A (Bioprocessing Ltd.). The fourth and fifth pannings were done conventionally with 0.1 M HCl-glycine, pH2.2, containing 1mg of BSA per ml as the eluent.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>2500</BiopanningDataSetID>
<Peptides>CPSWWPVNC(2)
CPGWWPYPC(2)
CPDWWPYLC(1)</Peptides>
<Motif>P-x-W(2)-P-x(2)</Motif>
<Unique_Sequence_Number>3</Unique_Sequence_Number>
<Experimental_Method>Phage display (competitive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:9094664</Reference>
<Target_Name>Puumala virus</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>CX7C phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>The panning included one antibody and two acid elution rounds. All solutions were made with Dul-becco's salt solution containing Ca2+ and Mg2+ (panning, washing, and antibody elution). In the first and second pannings, the phages were allowed to bind to Puumala virus in a solution containing 0.33% BSA. In the first panning, MAb 5B7 was used in the preelution, followed by MAb 1C9 elution, and the well was washed with a 1% BSA solution and then without BSA. Any residual MAb was removed from the amplification product of the first panning with Prosep A. In the second panning, the phages were eluted with a low pH. The third panning was done with Puumala virus-infected cell extract. The extract was diluted 2:3 in phosphate-buffered saline (PBS) containing 0.05% Tween20 (PBST) and 0.5% BSA and captured in a microtiter well coated with MAb 5B7 (5 mg/ml). The phages were added to the well in a solution containing 0.45% BSA and 40 mg of MAb 5A2 per ml, and the well was washed with 0.05% Tween 20. Low-pH elution was then performed.</Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item></BiopanningDataSet></result>