1301 CRGWRGEKIGNC CNMQALSMPVTC 2 Phage display (competitive panning) 5 PMID:20129923 Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1 Heparin Not determined. Not determined. CX10C T7 phage display library The library was biopanned against a chimera of mNdst1 consisting of the full-length protein minus the cytoplasmic tail and transmembrane domain fused to protein A. mNdst1 was immobilized on IgG beads, and heparin was used to displace bound phage. Both peptides inhibited mNdst1 activity in vitro, however, by distinct mechanisms. The peptide CRG WRGEKIGNC presents a chemokine-like repeat motif (BXX, where B represents a basic amino acid and X is a noncharged amino acid) and binds to heparan sulfate, thus blocking the binding of substrate to the enzyme. The peptide NMQALSMPVT inhibits mNdst1 activity by direct interaction with the enzyme near the active site. 1302 SNFYMPL(48) 1 Phage display (subtractive panning) 4 PMID:20637198 Human OE33 (esophageal adenocarcinoma) cells Not determined. Not determined. Not determined. Ph.D.-7 phage display library (X7) Peptide selection was performed using phage display by removing nonspecific binders using Q-hTERT (intestinal metaplasia) cells and achieving specific binding against OE33 (esophageal adenocarcinoma) cells. After completion of biopanning, plaques from a total of 60 phage that demonstrated preferential binding to the OE33 cells were selected. Authors found that 48 of these 60 clones (80%) contained the identical DNA sequence and corresponded to the peptide with amino acid sequence SNFYMPL. The other 12 clones expressed different unique amino acid sequences. The peptide sequence SNFYMPL binds specifically to dysplasia in Barrett's esophagus and can be fluorescence labeled to target premalignant mucosa on imaging. 1303 HKTTLSPASH(1) HKTASTPATH(1) PRFSTTPASH(1) AKGNTAPATD(1) NNSSAAPATQ(1) RFPTAAPATA(1) TKSYIAAPAS(5) TXSYIAAPAS(1) GKYFTAAPAS(1) LKTLMTAPAT(1) FPDPPTAPAT(1) LARPNVAPAT(1) FSPLNWPSAT(1) AATPRAYAPAS(1) ARPAPATYG(1) HNMAPATLH(1) HPWKQEAAPAS(1) LRPAPASVI(1) HCAAPASRQ(1) APATHLPAQ(1) VTASPATLFG(1) SSPPASIHSL(1) I-A(2)-P-A-[ST] 22 Phage display (common panning) 3 PMID:20699234 Lupus-derived monoclonal antibody BT164 Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) After three panning rounds a consensus was obtained with sequence IAAPAS/T corresponding to amino acids 27-KSAPAT-32 from histone H3. 1304 HTDWRLGTWHHS(3) NWITMNPAMPTL(6) LPFNTLADPRIN(5) LLADTTHHRPWT(5) NLLIPENVPLRH(1) 5 Phage display (common panning) 5 PMID:20949958 Hyperbranched poly(phenylene vinylene) (hypPPV) Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) 1305 ELWSIDTSAHRK(6) YYPASSTIQSRP(2) HPTLHMTYYKKQ(1) HIHRGEHGPSAR(5) TPLTPNGLTRSG(2) IVKNVPLTPLRE(1) AVPHRVGGLHSL(1) NYLHNHPYGTVG(1) EHPHVPITPSNL(1) 9 Phage display (common panning) 5 PMID:20949958 Linear poly(phenylene vinylene) (linPPV) Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) 1306 AFTHEAPKRRDS(4) SFPGPASARAGA(13) QIEESFVRGJTT(1) SLYKLRNVAAGR(2) CRWSTPTTSQCP(1) IHWSWTTVERPH(3) WPANILSHGPKH(1) 7 Phage display (common panning) 5 PMID:21131596 Apoptosis regulator Bcl-2 Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) At the final round, bound phages were eluted by addition of excess amount of Bcl-2 protein. Authors showed that the P6 peptide specifically recognized binding to the Bcl-2 protein in the cell system (in vivo). 1307 EHWSHDMFSPGD(9) EVSLHDMNLATH(2) KWLGHDMIMSGT(1) FNTKHDMQGDTS(1) EHNDFPMYTWRP(1) TTTHFLATKFYK(1) E-x(3)-H-D-M 6 Phage display (common panning) 3 PMID:21118490 Anti-urease B monoclonal antibody U001 Urease subunit beta Not determined. Not determined. Ph.D.-12 phage display library (X12) EXXXHDM matched the urease B proteins at 347-353 aa. 1308 CEKLKHSMC(10) CTKTWQSMC(2) CMSLLGHKC(1) CKHGLLSMC(1) CMSQDGHTC(1) E-x(3)-H-S-M 5 Phage display (common panning) 3 PMID:21118490 Anti-urease B monoclonal antibody U001 Urease subunit beta Not determined. Not determined. Ph.D.-C7C phage display library (CX7C) EXXXHSM matched the urease B proteins at 347-353 aa. 1309 STLMTTTYHSVS(1) QGAHYEYSRTEL(1) IPGDAGKGLHMT(1) YDTTSSPPRLTR(1) GMIKAAHERPLR(1) VLSNSLPTAIST(1) GMATEATVHELA(1) LIRGLLIGFGRN(1) YPLLPESPTDAN(2) NWSAEKAKLYDS(1) QNSHRVALENNT(1) 11 Phage display (common panning) 3 PMID:21234986 Indium nitride (InN) semiconductor (SC) material Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) Prior to the phage display, the InN surfaces were preliminarily prepared by appropriate chemical etching; thus, native oxides have been removed assuring the specific phage to reach the SC. As the YPLLPESPTDAN appears two times over 12, this peptide can be expected to be a good binder. 1310 SATTHYRLQAAN(11) TEHPSNTSPMRL(2) SGNTHYRLQAAN(1) TPHRLDWSPHLV(1) 4 Phage display (common panning) 4 PMID:21151669 Fibrosarcoma cell line NG4TL4-tk Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) A 12-mer amino acid peptide SATTHYRLQAAN, denominated TK4, was isolated from a phage-display library with fibrosarcoma tumor-binding activity. In vivo biodistribution analysis of TK4-displaying phage showed a significant increased phage titer in implanted tumor up to 10-fold in comparison with normal tissues after systemic administration in mouse. 1311 CAYHRLRRC(55) CGFYWLRSC(5) CSFFYLRSC(16) R-L-R(2), F-[FY]-x-L-R-S 3 Phage display (common panning) 4 PMID:21063027 Human leukemia cells MOLT-4 Not determined. Not determined. Not determined. fUSE5-based CX7C phage display library Phage selection was performed with an excess of the competing Arg-Gly-Asp (RGD) synthetic integrin-binding peptide motif to minimize and eliminate the recovery of RGD-containing ligands. By screening of human leukemia cells with a combinatorial phage display peptide library, Authors isolated a peptide motif, sequence Phe-Phe/Tyr-Any-Leu-Arg-Ser (FF/YXLRS), which bound to different leukemia cell lines and to patient-derived bone marrow samples. 1312 CAVTDGKQC(5) CQRPPR(4) CRPAR(4) CRPPR(2) CKPPR(1) CKAPR(1) CGRQGAR(2) CTLTGNSKC(2) CASLVLVAC(2) CKPPTPEEC(1) CRPAVRISC(1) CSYTKDKTC(1) CSHDA(1) CQSVRG(1) 14 Phage display (subtractive panning) 2-3 PMID:20869411 Macrophages isolated from primary human lung squamous carcinoma Not determined. Not determined. Not determined. Byungheon Lee (Department of Biochemistry and Cell Biology, School Medicine, Kyungpook National University, Republic of Korea) For subtraction, the eluted phage solution was incubated with cells from normal tissue and then the supernatant containing unbound phages was recovered. Using phage display, Authors identified the CQRPPR peptide, named ApoPep-1(Apoptosis-targeting Peptide-1), that was able to home to apoptotic and necrotic cells in tumor tissue. ApoPep-1 also bound to apoptotic and necrotic cells in culture, while only little binding to live cells was observed. Its binding to apoptotic cells was not dependent on calcium ion and not competed by annexin V. 1313 TIPKWISIIQALR(94) 1 Phage display (common panning) 3 PMID:21093050 Peptide SLGLSFYQPPEGDNALC Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) The selected phage population was screened further by affinity chromatography using PMCA from rabbit duodenal mucosa which expressed mostly PMCA1. Following competition, 184 plaques were picked and their plasmid DNA was sequenced. The dominant phage clone had 94 copies and encoded for a variable peptide sequence TIPKWISIIQALR. 1314 SFHQLPARSPLP GSTQAWMSPPLA LLADTTHHRPWT 3 Phage display (subtractive panning) 3 PMID:20952686 In vitro M cell coculture system Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) Negative panning was performed to remove the phage particles displaying peptides capable of binding to the monocultured Caco-2 cells. On the basis of the deduced amino acid sequences of these peptides, authors selected three peptides because these sequences were found at least four times and were not found in the sequences from phage particles that bound to monocultured Caco-2 cells. One of the selected peptide ligands, SFHQLPARSPLP, promoted the binding of ligand-fused Ag to mouse Peyer's patch M cells and human M-like cells that had been defined by binding with the M cell-specific and anti-GP2 Abs. 1315 QTYTPTKQSPPMPRP YLRITSTPHKYLTQR IKAPNPPSVSTLPPR RKRAPPPALRTAPRS PRDSMLFMPCKFRPM PVLIFKKIVLTAPVA AKPLASPRETGASQR RKSLPIALQLHHSYN QSPSCHMSSLQCTQL KLVCVSANFQSGVPH SRLTRNDMVTGCMC HVTSTKAWYDPSQPL RAKASATVCHLSNPY PMRPKGPDTLLYTLP VILNWRPSCLVTCHE KEMVVSCPPGALAYS MNRLPDFTRLPPYSP ANGVPIPPHPARAAR KGMRMRLAIGPDSA RPKLLHCEPSPAVVQ QSGMPQCYTALRPRV TPGLDAAVFWSLGSE LVIAPMCKPPPYTPE QHTLIIDATMPSASP RVMKHRTPSSRYQKP TNSSRPLSKSRQYRC KDPALLTRSPPSARM TSMIYRPHNVQTLLH APSGFARRTQTFWYV 29 Phage display (subtractive panning, in vivo) 4 PMID:20958260 PC-3 human prostate carcinoma cell Not determined. Not determined. Not determined. f88-15mer phage display library (X15) The library was precleared of phage that bound to the vasculature and other non-tumor antigens in normal non-tumor bearing CF1 mice, and then utilized in an in vivo selection scheme in PC-3 human prostate tumor-bearing mice. 1316 INTECAGLGLVCKPHT NKSKCRCRQNACKQLI CTSSCKPHSQSCKEKT NKKQCKTVLKMCHRRV DRPHCLKTWNICTSYY MKRECKNRCALCKSER IVPGCSKTERGCSYQS DMASCTQHADNWLKHE KPSPCSSFKSHCVRRD AKYYCEELVNHCTSAQ GDLRCRITKQKCEQQC ETIMCIRYRCDCPLPH GPAHCKRTISQCQTNE DEWHCKFNGAVCTSMR TPILCENIRSGCELKR QRVTCDMAENCCPKTS TNTECNTLSKLCQSSI HMQVCATVTHQCWIYG PPRLCQGMRGTCSGNQ CACICPCNPAFCTVAV KMPECHEQQEYCDGDR QKEHCILHTANCGRIT TNTNCGTDLEPCVSTM LKGDCTQRYVYCMKSK HDKQCLTAKDRCGTIK GDSSCQEVQTQCRYSK ASCECNPHPRHCGETR 27 Phage display (subtractive panning, in vivo) 4 PMID:20958260 PC-3 human prostate carcinoma cell Not determined. Not determined. Not determined. f88-Cys6 phage display library (X4CX6CX4) The library was precleared of phage that bound to the vasculature and other non-tumor antigens in normal non-tumor bearing CF1 mice, and then utilized in an in vivo selection scheme in PC-3 human prostate tumor-bearing mice. 1317 RAPMGGR RRPVGRA RLPPKAG RRPVVGR RAPARRY SRPGLRR VGPRTLR RGPRGRV 8 Phage display (common panning) 5 PMID:21071869 Soluble 37/48kDa oligomer formation of Aβ(1-42) Not determined. Not determined. Not determined. T7 phage display library (X2PX4) Although the reason for the enrichment of the arginine residues is not fully understood, highly cationic sequences containing at least three arginine residues are probably important in binding to the soluble Aβ(1-42) structure, because arginine contains a basic guanidine group. These peptides were found to suppress specifically 37/48kDa oligomer formation and to keep the monomeric form of Aβ(1-42) even after 24h of incubation, as disclosed by SDS-PAGE and size-exclusion chromatography. 1318 CGSYGFNAC(3) CSLERLGFC(7) CYRLTGLWC(2) CLDSASRGC(2) CGLRLESTC(2) CWLFSVSAC(2) 6 Phage display (common panning) 2-3 PMID:21070862 Virulent isolate of Paracoccidioides brasiliensis (Pb18) Not determined. Not determined. Not determined. CX7C fUSE5 phage display library Variability of CGSYGFNAC phage binding to different Pb isolates were examples of variability of expression by the fungus of its binding molecule, strongly suggesting CGSYGFNAC as a biomarker of virulence. 1319 CTSGTHPRC 1 Phage display (common panning) 4 PMID:21182881 Primary rat lung alveolar epithelial primary cell cultures Not determined. Not determined. Not determined. Ph.D.-C7C phage display library (CX7C) The first three-rounds identified apical cell-surface binders, while the 4th round aimed to identify phage internalised by the ATI-like cells. Peptide CTSGTHPRC showed significant pulmonary epithelial translocation across highly restrictive polarised cell monolayers. Cell biological data supported a differential alveolar epithelial cell interaction of the CTSGTHPRC peptide-phage clone and the corresponding free synthetic CTSGTHPRC peptide. 1320 GWWYKGRARPVSAVA(15) RAVWRHSVATPSHSV(7) LWRPVLFHSAVRALG(1) WRGVYFGDRWLGSQP(1) GWYSSRHYVRSLNGL(1) QQLVYNWWAVSSARR(1) LSWPLHAGRGFRWVS(1) 7 Phage display (common panning) 4 PMID:19558186 Ganglioside GM3 Not determined. Not determined. Not determined. fUSE5-based X15 phage display library The peptides were found to have affinity for GM3, and alanine scanning showed seven amino acid residues that contribute to carbohydrate recognition. The binding of peptides to the cell surface was significantly inhibited in the presence of sialic acid or by the digestion of cell surface sialyl residues by neuraminidase. 1321 EPWLDSRYSPLS GHGLLQYTDVMF TSLYTDRPSTPL LPIPSSLGGPFP SYEMPFSTRPWF LPGWPLAERVGQ TGHQSPGAYAAH NFMESLPRLGMH HSTWKLLRLDME HATGTHGLSLSH SFLYSYTGPRPL TMGFTAPRFPHY SLKMPHWPHLLP KAWIVQPPFHYS QLPKHNYWPGAF YTTSNTLQVIAR NTPGIRPQATYS ALHPLTNRHYAT SNTSIIRNAFPQ GVSQNTNSLHLR GMVSTSRMHAGW 21 Phage display (common panning) 4 PMID:15278181 Germania Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) The powder was exposed to the phage library, after which the powder was washed repeatedly to remove any free phage particles. The bound phage were then eluted by incubation glycine-HCl solution. The 3 most dominant peptides identified from the clones were chosen for further evaluation. The extent of germania precipitation (i.e. the germania precipitating activity) was quantified by adapting the β-silicomolybdate colorimetric assay. SLKMPHWPHLLP and TGHQSPGAYAAH peptides exhibited relatively high germania-precipitating activities, whereas the TSLYTDRPSTPL peptide exhibited much lower activity. 1322 NLLMAAS KLWVIPK HHHRHSF HPWLTRH 4 Phage display (common panning) PMID:14978510 Extracellular domain of Tie2 Not determined. Not determined. Not determined. Ph.D.-7 phage display library (X7) In fact, the target is Tie2-Fc. At the end of the selection, 48 clones were isolated and sequenced, showing that 11 different peptides were represented. Each selected clone was assayed by ELISA for binding to Tie2-Fc. Four clones gave the highest signal. One peptide, NLLMAAS, completely abolished the binding to Tie2 of both angiopoietin 2 and angiopoietin 1 (Ang1). We further show that NLLMAAS specifically suppresses both Ang1-induced ERK activity and migration in human umbilical endothelial cells. Moreover, in vivo, this peptide inhibits angiogenesis in the chick chorioallantoic membrane assay. 1323 GALTPLR(1) SYTPLRP(1) GFTPHRS(1) AIETLIR(1) NYYTPHR(1) HTQTRHR(1) NDLTPLR(1) SPFTPHR(1) SYTPHRT(1) T-x(2)-R 9 Phage display (common panning) 3 PMID:18400009 Anti-M2e monoclonal antibody 8C6 Matrix protein 2 Not determined. Not determined. Ph.D.-7 phage display library (X7) The phage clones exhibited a consensus motif (TXXR), which was found on the epitope EVETPIRN on influenza A virus M2 protein. Site-directed mutation analysis indicated that Thr and Arg on the epitope EVETPIRN played a key role in the recognition by 8C6. Furthermore, sequence alignment and analysis revealed that Thr and Arg on the epitope were highly conserved. 1324 WGRFWGRWLA(5) VCDWWGWGIC(3) YWMGWKWEGE(6) WWDFLQGSER(1) FAMWYPLGWR(1) W-x(2)-W 5 Phage display (competitive panning) 5 PMID:9492279 Doxorubicin P-glycoprotein Not determined. Not determined. fUSE5-based X10 phage display library To ensure a high level of the drug absorption on polysterene, doxorubicin was conjugated to BSA, and the conjugate was immobilized on polystyrene ELISA plates. Displacement with verapamil, a competitive inhibitor of doxorubicin binding with P-glycoprotein were used to elute the phages that bound to the doxorubicin-BSA2-coated plates. The displacement assay showed that the phages expressing these peptides bound MDR type drugs (vinblastine, doxorubicin, verapamil, and genistein) with the same selectivity as P-glycoprotein and did not interact with non-MDR type drugs, such as arabinosylcytosine (Ara-C) and melphalan. The structure modeling suggested that all the selected sequences contained a hydrophobic envelope in which MDR drugs could be docked with substantial energy minimization. 1325 TWWWTWAGKH(1) LWSPWYGGSW(9) W-x(2)-W 2 Phage display (common panning) 4 PMID:9492279 Doxorubicin P-glycoprotein Not determined. Not determined. fUSE5-based X10 phage display library To ensure a high level of the drug absorption on polysterene, doxorubicin was conjugated to BSA, and the conjugate was immobilized on polystyrene ELISA plates. Treatment with low-pH buffer which is usually used for phage panning were used to elute the phages that bound to the doxorubicin-BSA2-coated plates. The displacement assay showed that the phages expressing these peptides bound MDR type drugs (vinblastine, doxorubicin, verapamil, and genistein) with the same selectivity as P-glycoprotein and did not interact with non-MDR type drugs, such as arabinosylcytosine (Ara-C) and melphalan. The structure modeling suggested that all the selected sequences contained a hydrophobic envelope in which MDR drugs could be docked with substantial energy minimization.