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Potential of phage-displayed peptide library technology to identify functional targeting peptides

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Pages 525-537 | Published online: 14 May 2007

Bibliography

  • KRUMPE LR, MORI T: The use of phage-displayed peptide libraries to develop tumor-targeting drugs. Int. J. Peptide Res. Ther. (2006) 12(1):79-91.
  • MORI T: Cancer-specific ligands identified from screening of peptide-display libraries. Curr. Pharm. Des. (2004) 10(19):2335-2343.
  • BRISSETTE R, PRENDERGAST JK, GOLDSTEIN NI: Identification of cancer targets and therapeutics using phage display. Curr. Opin. Drug Discov. Dev. (2006) 9(3):363-369.
  • ROWLEY MJ, O’CONNOR K, WIJEYEWICKREMA L: Phage display for epitope determination: a paradigm for identifying receptor–ligand interactions. Biotechnol. Ann. Rev. (2004) 10:151-188.
  • MULLEN LM, NAIR SP, WARD JM, RYCROFT AN, HENDERSON B: Phage display in the study of infectious diseases. Trends Microbiol. (2006) 14(3):141-147.
  • FAN Q, LEUTHER KK, HOLMES CP et al.: Preclinical evaluation of Hematide, a novel erythropoiesis stimulating agent, for the treatment of anemia. Exp. Hematol. (2006) 34(10):1303-1311.
  • WARK PA: DX-890 (Dyax). IDrugs (2002) 5(6):586-589.
  • OLINER J, MIN H, LEAL J et al.: Suppression of angiogenesis and tumor growth by selective inhibition of angiopoietin-2. Cancer Cell (2004) 6(5):507-516.
  • BUSSEL JB, KUTER DJ, GEORGE JN et al.: AMG 531, a thrombopoiesis-stimulating protein, for chronic ITP. N. Engl. J. Med. (2006) 355(16):1672-1681.
  • SALMON SE, LAM KS, FELDER S et al.: One bead, one chemical compound: use of the selectide process for anticancer drug discovery. Acta Oncol. (1994) 33(2):127-131.
  • CHEN X, GAMBHIR SS: Significance of one-bead-one-compound combinational chemistry. Nat. Chem. Biol. (2006) 2(7):351-352.
  • LAM KS, LEBL M, KRCHNAK V: The ‘one-bead-one-compound’ combinatorial library method. Chem. Rev. (1997) 97(2):411-448.
  • WILSON DS, KEEFE AD, SZOSTAK JW: The use of mRNA display to select high-affinity protein-binding peptides. Proc. Natl. Acad. Sci. USA (2001) 98(7):3750-3755.
  • NEMOTO N, MIYAMOTO-SATO E, HUSIMI Y, YANAGAWA H: In vitro virus: bonding of mRNA bearing puromycin at the 3′-terminal end to the C-terminal end of its encoded protein on the ribosome in vitro. FEBS Lett. (1997) 414(2):405-408.
  • ROBERTS RW, SZOSTAK JW: RNA-peptide fusions for the in vitro selection of peptides and proteins. Proc. Natl. Acad. Sci. USA (1997) 94(23):12297-12302.
  • YONEZAWA M, DOI N, KAWAHASHI Y, HIGASHINAKAGAWA T, YANAGAWA H: DNA display for in vitro selection of diverse peptide libraries. Nucleic Acids Res. (2003) 31(19):e118.
  • MATTHEAKIS LC, BHATT RR, DOWER WJ: An in vitro polysome display system for identifying ligands from very large peptide libraries. Proc. Natl. Acad. Sci. USA (1994) 91(19):9022-9026.
  • HANES J, PLUCKTHUN A: In vitro selection and evolution of functional proteins by using ribosome display. Proc. Natl. Acad. Sci. USA (1997) 94(10):4937-4942.
  • LAMLA T, ERDMANN VA: Searching sequence space for high-affinity binding peptides using ribosome display. J. Mol. Biol. (2003) 329(2):381-388.
  • BESSETTE PH, RICE JJ, DAUGHERTY PS: Rapid isolation of high-affinity protein binding peptides using bacterial display. Prot. Eng. Des. Sel. (2004) 17(10):731-739.
  • RICE JJ, SCHOHN A, BESSETTE PH, BOULWARE KT, DAUGHERTY PS: Bacterial display using circularly permuted outer membrane protein OmpX yields high affinity peptide ligands. Protein Sci. (2006) 15(4):825-836.
  • LU Z, MURRAY KS, VAN CLEAVE V et al.: Expression of thioredoxin random peptide libraries on the Escherichia coli cell surface as functional fusions to flagellin: a system designed for exploring protein-protein interactions. Biotechnology (N Y) (1995) 13(4):366-372.
  • WATERKAMP DA, MULLER OJ, YING Y, TREPEL M, KLEINSCHMIDT JA: Isolation of targeted AAV2 vectors from novel virus display libraries. J. Gene Med. (2006) 8(11):1307-1319.
  • MULLER OJ, KAUL F, WEITZMAN MD et al.: Random peptide libraries displayed on adeno-associated virus to select for targeted gene therapy vectors. Nat. Biotechnol. (2003) 21(9):1040-1046.
  • MAKELA AR, OKER-BLOM C: Baculovirus display: a multifunctional technology for gene delivery and eukaryotic library development. Adv. Virus Res. (2006) 68:91-112.
  • SCOTT JK, SMITH GP: Searching for peptide ligands with an epitope library. Science (1990) 249(4967):386-390.
  • DEVLIN JJ, PANGANIBAN LC, DEVLIN PE: Random peptide libraries: a source of specific protein binding molecules. Science (1990) 249(4967):404-406.
  • SMITH GP: Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface. Science (1985) 228(4705):1315-1317.
  • LADNER RC, SATO AK, GORZELANY J, DE SOUZA M: Phage display-derived peptides as therapeutic alternatives to antibodies. Drug Discov. Today (2004) 9(12):525-529.
  • MORI T: Cancer-specific ligands identified from screening of peptide-display libraries. Curr. Pharm. Des. (2004) 10(19):2335-2343.
  • SZARDENINGS M: Phage display of random peptide libraries: applications, limits, and potential. J. Recept. Signal Transduct. Res. (2003) 23(4):307-349.
  • RUOSLAHTI E, DUZA T, ZHANG L: Vascular homing peptides with cell-penetrating properties. Curr. Pharm. Des. (2005) 11(28):3655-3660.
  • PASCHKE M: Phage display systems and their applications. Appl. Microbiol. Biotechnol. (2006) 70(1):2-11.
  • KEHOE JW, KAY BK: Filamentous phage display in the new millennium. Chem. Rev. (2005) 105(11):4056-4072.
  • RODI DJ, SOARES AS, MAKOWSKI L: Quantitative assessment of peptide sequence diversity in M13 combinatorial peptide phage display libraries. J. Mol. Biol. (2002) 322(5):1039-1052.
  • KRUMPE LR, ATKINSON AJ, SMYTHERS GW et al.: T7 lytic phage-displayed peptide libraries exhibit less sequence bias than M13 filamentous phage-displayed peptide libraries. Proteomics (2006) 6(15):4210-4222.
  • ZUCCONI A, DENTE L, SANTONICO E, CASTAGNOLI L, CESARENI G: Selection of ligands by panning of domain libraries displayed on phage lambda reveals new potential partners of synaptojanin 1. J. Mol. Biol. (2001) 307(5):1329-1339.
  • LINDQVIST BH, NADERI S: Peptide presentation by bacteriophage P4. FEMS Microbiol. Rev. (1995) 17(1-2):33-39.
  • GARUFI G, MINENKOVA O, LO PASSO C, PERNICE I, FELICI F: Display libraries on bacteriophage lambda capsid. Biotechnol. Ann. Rev. (2005) 11:153-190.
  • LIANG S, LIN T, DING J et al.: Screening and identification of vascular-endothelial-cell-specific binding peptide in gastric cancer. J. Mol. Med. (2006) 84(9):764-773.
  • BRATKOVIC T, LUNDER M, POPOVIC T et al.: Affinity selection to papain yields potent peptide inhibitors of cathepsins L, B, H, and K. Biochem. Biophys. Res. Commun. (2005) 332(3):897-903.
  • AGGARWAL S, HARDEN JL, DENMEADE SR: Synthesis and screening of a random dimeric peptide library using the one-bead-one-dimer combinatorial approach. Bioconjug. Chem. (2006) 17(2):335-340.
  • DING H, PRODINGER WM, KOPECEK J: Two-step fluorescence screening of CD21-binding peptides with one-bead one-compound library and investigation of binding properties of N-(2-hydroxypropyl)methacrylamide copolymer-peptide conjugates. Biomacromolecules (2006) 7(11):3037-3046.
  • KOOLPE M, BURGESS R, DAIL M, PASQUALE EB: EphB receptor-binding peptides identified by phage display enable design of an antagonist with ephrin-like affinity. J. Biol. Chem. (2005) 280(17):17301-17311.
  • HEKIM C, LEINONEN J, NARVANEN A et al.: Novel peptide inhibitors of human kallikrein 2. J. Biol. Chem. (2006) 281(18):12555-12560.
  • GARCES CA, KURENOVA EV, GOLUBOVSKAYA VM, CANCE WG: Vascular endothelial growth factor receptor-3 and focal adhesion kinase bind and suppress apoptosis in breast cancer cells. Cancer Res. (2006) 66(3):1446-1454.
  • DING H, PRODINGER WM, KOPECEK J: Identification of CD21-binding peptides with phage display and investigation of binding properties of HPMA copolymer-peptide conjugates. Bioconjug. Chem. (2006) 17(2):514-523.
  • LI B, RUSSELL SJ, COMPAAN DM et al.: Activation of the proapoptotic death receptor DR5 by oligomeric peptide and antibody agonists. J. Mol. Biol. (2006) 361(3):522-536.
  • CHANG CY, ABDO J, HARTNEY T, MCDONNELL DP: Development of peptide antagonists for the androgen receptor using combinatorial peptide phage display. Mol. Endocrinol. (2005) 19(10):2478-2490.
  • POND CD, MARSHALL KM, BARROWS LR: Identification of a small topoisomerase I-binding peptide that has synergistic antitumor activity with 9-aminocamptothecin. Mol. Cancer Ther. (2006) 5(3):739-745.
  • BIKKAVILLI RK, TSANG SY, TANG WM et al.: Identification and characterization of surrogate peptide ligand for orphan G protein-coupled receptor mas using phage-displayed peptide library. Biochem. Pharmacol. (2006) 71(3):319-337.
  • OYAMA T, ROMBEL IT, SAMLI KN, ZHOU X, BROWN KC: Isolation of multiple cell-binding ligands from different phage displayed-peptide libraries. Biosens. Bioelectron. (2006) 21(10):1867-1875.
  • AINA OH, MARIK J, LIU R, LAU DH, LAM KS: Identification of novel targeting peptides for human ovarian cancer cells using ‘one-bead one-compound’ combinatorial libraries. Mol. Cancer Ther. (2005) 4(5):806-813.
  • DANE KY, CHAN LA, RICE JJ, DAUGHERTY PS: Isolation of cell specific peptide ligands using fluorescent bacterial display libraries. J. Immunol. Methods (2006) 309(1-2):120-129.
  • SHUKLA GS, KRAG DN: Selection of tumor-targeting agents on freshly excised human breast tumors using a phage display library. Oncol. Rep. (2005) 13(4):757-764.
  • KIM Y, LILLO AM, STEINIGER SC et al.: Targeting heat shock proteins on cancer cells: selection, characterization, and cell-penetrating properties of a peptidic GRP78 ligand. Biochemistry (2006) 45(31):9434-9444.
  • KOLONIN MG, BOVER L, SUN J et al.: Ligand-directed surface profiling of human cancer cells with combinatorial peptide libraries. Cancer Res. (2006) 66(1):34-40.
  • MAKELA AR, MATILAINEN H, WHITE DJ, RUOSLAHTI E, OKER-BLOM C: Enhanced baculovirus-mediated transduction of human cancer cells by tumor-homing peptides. J. Virol. (2006) 80(13):6603-6611.
  • WANG FY, ZHANG TY, LUO JX et al.: Selection of CC chemokine receptor 5-binding peptide from a phage display peptide library. Biosci. Biotechnol. Biochem. (2006) 70(9):2035-2041.
  • VYROUBALOVA EC, HARTLEY O, MERMOD N, FISCH I: Identification of peptide ligands to the chemokine receptor CCR5 and their maturation by gene shuffling. Mol. Immunol. (2006) 43(10):1573-1578.
  • ROBINSON P, STUBER D, DERYCKERE F et al.: Identification using phage display of peptides promoting targeting and internalization into HPV-transformed cell lines. J. Mol. Recognit. (2005) 18(2):175-182.
  • LUNDER M, BRATKOVIC T, KREFT S, STRUKELJ B: Peptide inhibitor of pancreatic lipase selected by phage display using different elution strategies. J. Lipid Res. (2005) 46(7):1512-1516.
  • DE J, CHANG YC, SAMLI KN et al.: Isolation of a mycoplasma-specific binding peptide from an unbiased phage-displayed peptide library. Mol. Biosyst. (2005) 1(2):149-157.
  • KIM YG, LEE CS, CHUNG WJ et al.: Selection of peptides for lipopolysaccharide binding on to epoxy beads and selective detection of Gram-negative bacteria. Biotechnol. Lett. (2006) 28(2):79-84.
  • NISHIKAWA K, WATANABE M, KITA E et al.: A multivalent peptide library approach identifies a novel Shiga toxin inhibitor that induces aberrant cellular transport of the toxin. FASEB J. (2006) Epub ahead of print.
  • PINI A, GIULIANI A, FALCIANI C et al.: Antimicrobial activity of novel dendrimeric peptides obtained by phage display selection and rational modification. Antimicrob. Agents Chemother. (2005) 49(7):2665-2672.
  • EDA K, EDA S, SHERMAN IW: Identification of peptides targeting the surface of Plasmodium falciparum-infected erythrocytes using a phage display peptide library. Am. J. Trop. Med. Hyg. (2004) 71(2):190-195.
  • KITAGAWA M, GOTO D, MAMURA M et al.: Identification of three novel peptides that inhibit CD40–CD154 interaction. Mod. Rheumatol. (2005) 15(6):423-426.
  • WHITE SJ, SIMMONDS RE, LANE DA, BAKER AH: Efficient isolation of peptide ligands for the endothelial cell protein C receptor (EPCR) using candidate receptor phage display biopanning. Peptides (2005) 26(7):1264-1269.
  • AMEMIYA K, NAKATANI T, SAITO A, SUZUKI A, MUNAKATA H: Hyaluronan-binding motif identified by panning a random peptide display library. Biochim. Biophys. Acta (2005) 1724(1-2):94-99.
  • ORNER BP, LIU L, MURPHY RM, KIESSLING LL: Phage display affords peptides that modulate beta-amyloid aggregation. J. Am. Chem. Soc. (2006) 128(36):11882-11889.
  • BERNTZEN G, BREKKE OH, MOUSAVI SA et al.: Characterization of an FcgammaRI-binding peptide selected by phage display. Prot. Eng. Des. Sel. (2006) 19(3):121-128.
  • ARAP W, KOLONIN MG, TREPEL M et al.: Steps toward mapping the human vasculature by phage display. Nat. Med. (2002) 8(2):121-127.
  • KRAG DN, FULLER SP, OLIGINO L et al.: Phage-displayed random peptide libraries in mice: toxicity after serial panning. Cancer Chemother. Pharmacol. (2002) 50(4):325-332.
  • KRAG DN, SHUKLA GS, SHEN GP et al.: Selection of tumor-binding ligands in cancer patients with phage display libraries. Cancer Res. (2006) 66(15):7724-7733.
  • SAMOYLOVA TI, MORRISON NE, GLOBA LP, COX NR: Peptide phage display: opportunities for development of personalized anti-cancer strategies. Anti-Cancer Agents Med. Chem. (2006) 6(1):9-17.
  • ZOU J, DICKERSON MT, OWEN NK, LANDON LA, DEUTSCHER SL: Biodistribution of filamentous phage peptide libraries in mice. Mol. Biol. Rep. (2004) 31(2):121-129.
  • ZHANG J, SPRING H, SCHWAB M: Neuroblastoma tumor cell-binding peptides identified through random peptide phage display. Cancer Lett. (2001) 171(2):153-164.
  • ASKOXYLAKIS V, ZITZMANN S, MIER W et al.: Preclinical evaluation of the breast cancer cell-binding peptide, p160. Clin. Cancer Res. (2005) 11(18):6705-6712.
  • AKITA N, MARUTA F, SEYMOUR LW et al.: Identification of oligopeptides binding to peritoneal tumors of gastric cancer. Cancer Sci. (2006) 97(10):1075-1081.
  • LI Z, ZHAO R, WU X et al.: Identification and characterization of a novel peptide ligand of epidermal growth factor receptor for targeted delivery of therapeutics. FASEB J. (2005) 19(14):1978-1985.
  • JIANG YQ, WANG HR, LI HP et al.: Targeting of hepatoma cell and suppression of tumor growth by a novel 12mer peptide fused to superantigen TSST-1. Mol. Med. (2006) Epub ahead of print.
  • DU B, QIAN M, ZHOU Z et al.: In vitro panning of a targeting peptide to hepatocarcinoma from a phage display peptide library. Biochem. Biophys. Res. Commun. (2006) 342(3):956-962.
  • PENG L, LIU R, MARIK J et al.: Combinatorial chemistry identifies high-affinity peptidomimetics against alpha4beta1 integrin for in vivo tumor imaging. Nat. Chem. Biol. (2006) 2(7):381-389.
  • LAM KS, SALMON SE, HERSH EM et al.: A new type of synthetic peptide library for identifying ligand-binding activity. Nature (1991) 354(6348):82-84.
  • BOCKMANN M, DROSTEN M, PUTZER BM: Discovery of targeting peptides for selective therapy of medullary thyroid carcinoma. J. Gene Med. (2005) 7(2):179-188.
  • BOCKMANN M, HILKEN G, SCHMIDT A et al.: Novel SRESPHP peptide mediates specific binding to primary medullary thyroid carcinoma after systemic injection. Hum. Gene Ther. (2005) 16(11):1267-1275.
  • ERIKSSON F, CULP WD, MASSEY R et al.: Tumor specific phage particles promote tumor regression in a mouse melanoma model. Cancer Immunol. Immunother. (2006) Epub ahead of print.
  • TANAKA S, PERO SC, TAGUCHI K et al.: Specific peptide ligand for Grb7 signal transduction protein and pancreatic cancer metastasis. J. Natl. Cancer Inst. (2006) 98(7):491-498.
  • PERO SC, OLIGINO L, DALY RJ et al.: Identification of novel non-phosphorylated ligands, which bind selectively to the SH2 domain of Grb7. J. Biol. Chem. (2002) 277(14):11918-11926.
  • HUANG C, LIU XY, REHEMTULLA A, LAWRENCE TS: Identification of peptides that bind to irradiated pancreatic tumor cells. Int. J. Radiat. Oncol. Biol. Phys. (2005) 62(5):1497-1503.
  • NEWTON JR, KELLY KA, MAHMOOD U, WEISSLEDER R, DEUTSCHER SL: In vivo selection of phage for the optical imaging of PC-3 human prostate carcinoma in mice. Neoplasia (2006) 8(9):772-780.
  • ZITZMANN S, KRAMER S, MIER W et al.: Identification of a new prostate-specific cyclic peptide with the bacterial FliTrx system. J. Nucl. Med. (2005) 46(5):782-785.
  • ZITZMANN S, MIER W, SCHAD A et al.: A new prostate carcinoma binding peptide (DUP-1) for tumor imaging and therapy. Clin. Cancer Res. (2005) 11(1):139-146.
  • ARAP W, PASQUALINI R, RUOSLAHTI E: Cancer treatment by targeted drug delivery to tumor vasculature in a mouse model. Science (1998) 279(5349):377-380.
  • PASQUALINI R, KOIVUNEN E, KAIN R et al.: Aminopeptidase N is a receptor for tumor-homing peptides and a target for inhibiting angiogenesis. Cancer Res. (2000) 60(3):722-727.
  • KOIVUNEN E, GAY DA, RUOSLAHTI E: Selection of peptides binding to the α5β1 integrin from phage display library. J. Biol. Chem. (1993) 268(27):20205-20210.
  • DUNEHOO AL, ANDERSON M, MAJUMDAR S et al.: Cell adhesion molecules for targeted drug delivery. J. Pharm. Sci. (2006) 95(9):1856-1872.
  • CURNIS F, GASPARRI A, SACCHI A et al.: Targeted delivery of IFNgamma to tumor vessels uncouples antitumor from counterregulatory mechanisms. Cancer Res. (2005) 65(7):2906-2913.
  • CURNIS F, SACCHI A, BORGNA L et al.: Enhancement of tumor necrosis factor alpha antitumor immunotherapeutic properties by targeted delivery to aminopeptidase N (CD13). Nat. Biotechnol. (2000) 18(11):1185-1190.
  • SACCHI A, GASPARRI A, GALLO-STAMPINO C et al.: Synergistic antitumor activity of cisplatin, paclitaxel, and gemcitabine with tumor vasculature-targeted tumor necrosis factor-alpha. Clin. Cancer Res. (2006) 12(1):175-182.
  • KOLONIN MG, SUN J, DO KA et al.: Synchronous selection of homing peptides for multiple tissues by in vivo phage display. FASEB J. (2006) 20(7):979-981.
  • YAO VJ, OZAWA MG, TREPEL M et al.: Targeting pancreatic islets with phage display assisted by laser pressure catapult microdissection. Am. J. Pathol. (2005) 166(2):625-636.
  • SAMLI KN, MCGUIRE MJ, NEWGARD CB, JOHNSTON SA, BROWN KC: Peptide-mediated targeting of the islets of Langerhans. Diabetes (2005) 54(7):2103-2108.
  • WORK LM, BUNING H, HUNT E et al.: Vascular bed-targeted in vivo gene delivery using tropism-modified adeno-associated viruses. Mol. Ther. (2006) 13(4):683-693.
  • ZHANG L, HOFFMAN JA, RUOSLAHTI E: Molecular profiling of heart endothelial cells. Circulation (2005) 112(11):1601-1611.
  • KELLY KA, ALLPORT JR, TSOURKAS A et al.: Detection of vascular adhesion molecule-1 expression using a novel multimodal nanoparticle. Circ. Res. (2005) 96(3):327-336.
  • KELLY KA, NAHRENDORF M, YU AM, REYNOLDS F, WEISSLEDER R: In vivo phage display selection yields atherosclerotic plaque targeted peptides for imaging. Mol. Imaging Biol. (2006) 8(4):201-207.
  • PILCH J, BROWN DM, KOMATSU M et al.: Peptides selected for binding to clotted plasma accumulate in tumor stroma and wounds. Proc. Natl. Acad. Sci. USA (2006) 103(8):2800-2804.
  • AINA OH, SROKA TC, CHEN ML, LAM KS: Therapeutic cancer targeting peptides. Biopolymers (2002) 66(3):184-199.
  • MURANAKA N, HOHSAKA T, SISIDO M: Four-base codon mediated mRNA display to construct peptide libraries that contain multiple nonnatural amino acids. Nucleic Acids Res. (2006) 34(1):e7.
  • TIAN F, TSAO ML, SCHULTZ PG: A phage display system with unnatural amino acids. J. Am. Chem. Soc. (2004) 126(49):15962-15963.
  • BORGHOUTS C, KUNZ C, GRONER B: Peptide aptamers: recent developments for cancer therapy. Expert Opin. Biol. Ther. (2005) 5(6):783-797.
  • GREGORIADIS G, JAIN S, PAPAIOANNOU I, LAING P: Improving the therapeutic efficacy of peptides and proteins: a role for polysialic acids. Int. J. Pharm. (2005) 300(1-2):125-130.
  • LANDON LA, DEUTSCHER SL: Combinatorial discovery of tumor targeting peptides using phage display. J. Cell. Biochem. (2003) 90(3):509-517.
  • FLEMING TJ, SACHDEVA M, DELIC M et al.: Discovery of high-affinity peptide binders to BLyS by phage display. J. Mol. Recognit. (2005) 18(1):94-102.
  • EICHLER J: Synthetic peptide arrays and peptide combinatorial libraries for the exploration of protein-ligand interactions and the design of protein inhibitors. Comb. Chem. High Throughput Screen. (2005) 8(2):135-143.

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