메뉴 건너뛰기




Volumn 5, Issue 4, 2010, Pages 563-574

Enhanced binding and killing of target tumor cells by drug-loaded liposomes modified with tumor-specific phage fusion coat protein

Author keywords

Breast cancer; Doxil ; Drug delivery; Landscape phage; Liposome; Major coat protein pVIII; Phage display; Tumor targeting

Indexed keywords

COAT PROTEIN; DOXORUBICIN; LIPOSOME; MACROGOL;

EID: 77953394893     PISSN: 17435889     EISSN: None     Source Type: Journal    
DOI: 10.2217/nnm.10.30     Document Type: Article
Times cited : (80)

References (30)
  • 3
    • 37249021356 scopus 로고    scopus 로고
    • Surface-active liposomes for targeted cancer therapy
    • Sofou S: Surface-active liposomes for targeted cancer therapy. Nanomedicine (Lond.) 2(5), 711-724 (2007).
    • (2007) Nanomedicine (Lond.) , vol.2 , Issue.5 , pp. 711-724
    • Sofou, S.1
  • 4
  • 7
    • 3042825003 scopus 로고    scopus 로고
    • Cancer-specific ligands identified from screening of peptide-display libraries
    • Mori T: Cancer-specific ligands identified from screening of peptide-display libraries. Curr. Pharm. Des. 10, 2335-2343 (2004).
    • (2004) Curr. Pharm. Des. , vol.10 , pp. 2335-2343
    • Mori, T.1
  • 9
    • 52049117189 scopus 로고    scopus 로고
    • Evolution of phage display: From bioactive peptides to bioselective nanomaterials
    • Petrenko VA: Evolution of phage display: from bioactive peptides to bioselective nanomaterials. Expert Opin. Drug Deliv. 5, 825-836 (2008).
    • (2008) Expert Opin. Drug Deliv. , vol.5 , pp. 825-836
    • Petrenko, V.A.1
  • 10
    • 33645466758 scopus 로고    scopus 로고
    • The use of phage-displayed peptide libraries to develop tumor-targeting drugs
    • Krumpe LR, Mori T: The use of phage-displayed peptide libraries to develop tumor-targeting drugs. Int. J. Pept. Res. Ther. 12, 79-91(2006).
    • (2006) Int. J. Pept. Res. Ther. , vol.12 , pp. 79-91
    • Krumpe, L.R.1    Mori, T.2
  • 11
    • 4644302286 scopus 로고    scopus 로고
    • Novel RGD lipopeptides for the targeting of liposomes to integrin-expressing endothelial and melanoma cells
    • Hölig P, Bach M, Volkel T et al.: Novel RGD lipopeptides for the targeting of liposomes to integrin-expressing endothelial and melanoma cells. Protein Eng. Des. Sel. 17, 433-441 (2004).
    • (2004) Protein Eng. Des. Sel. , vol.17 , pp. 433-441
    • Hölig, P.1    Bach, M.2    Volkel, T.3
  • 12
    • 36348935200 scopus 로고    scopus 로고
    • Peptide-mediated targeting to tumor blood vessels of lung cancer for drug delivery
    • Lee TY, Lin CT, Kuo SY, Chang DK, Wu HC : Peptide-mediated targeting to tumor blood vessels of lung cancer for drug delivery. Cancer Res. 67, 10958-10965 (2007).
    • (2007) Cancer Res , vol.67 , pp. 10958-10965
    • Lee, T.Y.1    Lin, C.T.2    Kuo, S.Y.3    Chang, D.K.4    Wu, H.C.5
  • 13
    • 41849127472 scopus 로고    scopus 로고
    • Multifunctional peptide-based nanosystems for improving delivery and molecular imaging
    • Emerich DF, Thanos CG: Multifunctional peptide-based nanosystems for improving delivery and molecular imaging. Curr. Opin. Mol. Ther. 10, 132-139 (2008).
    • (2008) Curr. Opin. Mol. Ther. , vol.10 , pp. 132-139
    • Emerich, D.F.1    Thanos, C.G.2
  • 15
    • 0028248239 scopus 로고
    • Cleavable signal peptides are rarely found in bacterial cytoplasmic membrane proteins
    • Broome-Smith JK, Gnaneshan S, Hunt LA et al.: Cleavable signal peptides are rarely found in bacterial cytoplasmic membrane proteins. Mol. Membr. Biol. 11, 3-8 (1994).
    • (1994) Mol. Membr. Biol. , vol.11 , pp. 3-8
    • Broome-Smith, J.K.1    Gnaneshan, S.2    Hunt, L.A.3
  • 16
    • 0029098779 scopus 로고
    • Major coat proteins of bacteriophage Pf3 and M13 as model systems for sec-independent protein transport
    • Kuhn A: Major coat proteins of bacteriophage Pf3 and M13 as model systems for sec-independent protein transport. FEMS Microbiol. Rev. 17, 185-190 (1995).
    • (1995) FEMS Microbiol. Rev. , vol.17 , pp. 185-190
    • Kuhn, A.1
  • 17
    • 0030050901 scopus 로고    scopus 로고
    • Thermodynamics of the membrane insertion process of the M13 procoat protein, a lipid bilayer traversing protein containing a leader sequence
    • Soekarjo M, Eisenhawer M, Kuhn A, Vogel H: Thermodynamics of the membrane insertion process of the M13 procoat protein, a lipid bilayer traversing protein containing a leader sequence. Biochemistry 35, 1232-1241 (1996).
    • (1996) Biochemistry , vol.35 , pp. 1232-1241
    • Soekarjo, M.1    Eisenhawer, M.2    Kuhn, A.3    Vogel, H.4
  • 18
    • 33747890567 scopus 로고    scopus 로고
    • Selection of tumor-binding ligands in cancer patients with phage display libraries
    • Krag DN, Shukla GS, Shen GP et al.: Selection of tumor-binding ligands in cancer patients with phage display libraries. Cancer Res. 66, 7724-7733 (2006).
    • (2006) Cancer Res , vol.66 , pp. 7724-7733
    • Krag, D.N.1    Shukla, G.S.2    Shen, G.P.3
  • 19
    • 0024332154 scopus 로고
    • Production of a viable variant of the M13 phage with a foreign peptide inserted into the basic coat protein
    • Il'ichev AA, Minenkova OO, Tat'kov SI et al.: Production of a viable variant of the M13 phage with a foreign peptide inserted into the basic coat protein. Dokl. Akad. Nauk. SSSR 307, 481-483 (1989).
    • (1989) Dokl. Akad. Nauk. SSSR , vol.307 , pp. 481-483
    • Il'Ichev, A.A.1    Minenkova, O.O.2    Tat'Kov, S.I.3
  • 20
    • 0029793463 scopus 로고    scopus 로고
    • A library of organic landscapes on filamentous phage
    • Petrenko VA, Smith GP, Gong X, Quinn T: A library of organic landscapes on filamentous phage. Protein Eng. 9, 797-801 (1996).
    • (1996) Protein Eng , vol.9 , pp. 797-801
    • Petrenko, V.A.1    Smith, G.P.2    Gong, X.3    Quinn, T.4
  • 22
    • 0033829057 scopus 로고    scopus 로고
    • Phages from landscape libraries as substitute antibodies
    • Petrenko VA, Smith GP: Phages from landscape libraries as substitute antibodies. Protein Eng. 13, 589-592 (2000).
    • (2000) Protein Eng , vol.13 , pp. 589-592
    • Petrenko, V.A.1    Smith, G.P.2
  • 23
    • 0024468872 scopus 로고
    • Aggregation-related conformational change of the membrane-associated coat protein of bacteriophage M13
    • Spruijt RB, Wolfs CJ, Hemminga MA: Aggregation-related conformational change of the membrane-associated coat protein of bacteriophage M13. Biochemistry 28, 9158-9165 (1989).
    • (1989) Biochemistry , vol.28 , pp. 9158-9165
    • Spruijt, R.B.1    Wolfs, C.J.2    Hemminga, M.A.3
  • 24
    • 34948876843 scopus 로고    scopus 로고
    • Enhanced cytotoxicity of monoclonal anticancer antibody 2C5-modified doxorubicin-loaded PEGylated liposomes against various tumor cell lines
    • Elbayoumi TA, Torchilin VP: Enhanced cytotoxicity of monoclonal anticancer antibody 2C5-modified doxorubicin-loaded PEGylated liposomes against various tumor cell lines. Eur. J. Pharm. Sci. 32(3), 159-168 (2007).
    • (2007) Eur. J. Pharm. Sci. , vol.32 , Issue.3 , pp. 159-168
    • Elbayoumi, T.A.1    Torchilin, V.P.2
  • 25
    • 0002013346 scopus 로고    scopus 로고
    • Filamentous phage biology
    • Barbas CF et al. (Eds). Cold Spring Harbor Laboratory Press, NY, USA
    • Webster R: Filamentous phage biology. In: Phage Display: A Laboratory Manual. Barbas CF et al. (Eds). Cold Spring Harbor Laboratory Press, NY, USA, 1.1-1.37 (2001).
    • (2001) Phage Display: A Laboratory Manual , pp. 11-137
    • Webster, R.1
  • 26
    • 4344704702 scopus 로고    scopus 로고
    • Structure determination of membrane proteins by NMR spectroscopy
    • Opella SJ, Marassi FM: Structure determination of membrane proteins by NMR spectroscopy. Chemical Rev. 104, 3587-3606 (2004).
    • (2004) Chemical Rev , vol.104 , pp. 3587-3606
    • Opella, S.J.1    Marassi, F.M.2
  • 27
    • 33646560648 scopus 로고    scopus 로고
    • Anchoring mechanisms of membrane-associated M13 major coat protein
    • Stopar D, Spruijt RB, Hemminga MA: Anchoring mechanisms of membrane-associated M13 major coat protein. Chem. Phys. Lipids 141, 83-93 (2006).
    • (2006) Chem. Phys. Lipids , vol.141 , pp. 83-93
    • Stopar, D.1    Spruijt, R.B.2    Hemminga, M.A.3
  • 28
    • 0030732352 scopus 로고    scopus 로고
    • Detergent-mediated reconstitution of a glycosyl-phosphatidylinositol- protein into liposomes
    • Angrand M, Briolay A, Ronzon F, Roux B: Detergent-mediated reconstitution of a glycosyl-phosphatidylinositol-protein into liposomes. Eur. J. Biochem. 250, 168-176 (1997).
    • (1997) Eur. J. Biochem. , vol.250 , pp. 168-176
    • Angrand, M.1    Briolay, A.2    Ronzon, F.3    Roux, B.4
  • 29
    • 0024291653 scopus 로고
    • Mechanisms of membrane protein insertion into liposomes during reconstitution procedures involving the use of detergents. 1. Solubilization of large unilamellar liposomes (prepared by reverse-phase evaporation) by triton X-100 octyl glucoside and sodium cholate
    • Paternostre MT, Roux M, Rigaud JL: Mechanisms of membrane protein insertion into liposomes during reconstitution procedures involving the use of detergents. 1. Solubilization of large unilamellar liposomes (prepared by reverse-phase evaporation) by triton X-100, octyl glucoside, and sodium cholate. Biochemistry 27, 2668-2677 (1988).
    • (1988) Biochemistry , vol.27 , pp. 2668-2677
    • Paternostre, M.T.1    Roux, M.2    Rigaud, J.L.3
  • 30
    • 0024291663 scopus 로고
    • Mechanisms of membrane protein insertion into liposomes during reconstitution procedures involving the use of detergents. 2. Incorporation of the light-driven proton pump bacteriorhodopsin
    • Rigaud JL, Paternostre MT, Bluzat A: Mechanisms of membrane protein insertion into liposomes during reconstitution procedures involving the use of detergents. 2. Incorporation of the light-driven proton pump bacteriorhodopsin. Biochemistry 27, 2677-2688 (1988).
    • (1988) Biochemistry , vol.27 , pp. 2677-2688
    • Rigaud, J.L.1    Paternostre, M.T.2    Bluzat, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.