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Volumn 21, Issue 11, 2010, Pages 2055-2064

Synthesis, characterization, and thermodynamic study of a polyvalent lytic peptide-polymer conjugate as novel anticancer agent

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; LIPID BILAYERS; PEPTIDES;

EID: 78649270296     PISSN: 10431802     EISSN: 15204812     Source Type: Journal    
DOI: 10.1021/bc1002899     Document Type: Article
Times cited : (9)

References (26)
  • 1
    • 0036364467 scopus 로고    scopus 로고
    • Multidrug resistance in cancer: Role of ATP-dependent transporters
    • Gottesman, M. M., Fojo, T., and Bates, S. E. (2002) Multidrug resistance in cancer: Role of ATP-dependent transporters Nat. Rev. Cancer 2, 48-58
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 48-58
    • Gottesman, M.M.1    Fojo, T.2    Bates, S.E.3
  • 2
    • 33845699790 scopus 로고    scopus 로고
    • Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies
    • Hancock, R. E. W. and Sahl, H. G. (2006) Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies Nat. Biotechnol. 24, 1551-1557
    • (2006) Nat. Biotechnol. , vol.24 , pp. 1551-1557
    • Hancock, R.E.W.1    Sahl, H.G.2
  • 3
    • 3042737827 scopus 로고    scopus 로고
    • Membrane disrupting lytic peptides for cancer treatments
    • Leuschner, C. and Hansel, W. (2004) Membrane disrupting lytic peptides for cancer treatments Curr. Pharm. Des. 10, 2299-2310
    • (2004) Curr. Pharm. Des. , vol.10 , pp. 2299-2310
    • Leuschner, C.1    Hansel, W.2
  • 4
    • 18544366816 scopus 로고    scopus 로고
    • Host defense peptides as new weapons in cancer treatment
    • Papo, N. and Shai, Y. (2005) Host defense peptides as new weapons in cancer treatment Cell. Mol. Life Sci. 62, 784-790
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 784-790
    • Papo, N.1    Shai, Y.2
  • 5
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff, M. (2002) Antimicrobial peptides of multicellular organisms Nature 415, 389-395
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 6
    • 0036948138 scopus 로고    scopus 로고
    • Mode of action of membrane active antimicrobial peptides
    • Shai, Y. (2002) Mode of action of membrane active antimicrobial peptides Biopolymers 66, 236-248
    • (2002) Biopolymers , vol.66 , pp. 236-248
    • Shai, Y.1
  • 7
    • 0032693639 scopus 로고    scopus 로고
    • Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes
    • Matsuzaki, K. (1999) Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes Biochim. Biophys. Acta 1462, 1-10
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 1-10
    • Matsuzaki, K.1
  • 8
    • 0032476812 scopus 로고    scopus 로고
    • Polyvalent interactions in biological systems: Implications for design and use of multivalent ligands and inhibitors
    • Mammen, M., Choi, S. K., and Whitesides, G. M. (1998) Polyvalent interactions in biological systems: Implications for design and use of multivalent ligands and inhibitors Angew. Chem., Int. Ed. 37, 2755-2794
    • (1998) Angew. Chem., Int. Ed. , vol.37 , pp. 2755-2794
    • Mammen, M.1    Choi, S.K.2    Whitesides, G.M.3
  • 11
    • 0036183822 scopus 로고    scopus 로고
    • Antimicrobial dendrimeric peptides
    • Tam, J. P., Lu, Y. A., and Yang, J. L. (2002) Antimicrobial dendrimeric peptides Eur. J. Biochem. 269, 923-932
    • (2002) Eur. J. Biochem. , vol.269 , pp. 923-932
    • Tam, J.P.1    Lu, Y.A.2    Yang, J.L.3
  • 12
    • 77952575335 scopus 로고    scopus 로고
    • Tumor-selective delivery of macromolecular drugs via the EPR effect: Background and future prospects
    • Maeda, H. Tumor-selective delivery of macromolecular drugs via the EPR effect: background and future prospects, Bioconjugate Chem. 21, 797 - 802.
    • Bioconjugate Chem. , vol.21 , pp. 797-802
    • Maeda, H.1
  • 13
    • 0016636179 scopus 로고
    • An improved 2,4,6 trinitrobenzenesulfonic acid method for the determination of amines
    • Snyder, S. L. and Sobocinski, P. Z. (1975) An improved 2,4,6 trinitrobenzenesulfonic acid method for the determination of amines Anal. Biochem. 64, 284-288
    • (1975) Anal. Biochem. , vol.64 , pp. 284-288
    • Snyder, S.L.1    Sobocinski, P.Z.2
  • 14
    • 0031567121 scopus 로고    scopus 로고
    • Titration calorimetry of lipid-peptide interactions
    • Seelig, J. (1997) Titration calorimetry of lipid-peptide interactions Biochim. Biophys. Acta 1331, 103-116
    • (1997) Biochim. Biophys. Acta , vol.1331 , pp. 103-116
    • Seelig, J.1
  • 15
    • 0042884199 scopus 로고    scopus 로고
    • Antibacterial activity of short hydrophobic and basic-rich peptides
    • Chen, P. W., Shyu, C. L., and Mao, F. C. (2003) Antibacterial activity of short hydrophobic and basic-rich peptides Am. J. Vet. Res. 64, 1088-1092
    • (2003) Am. J. Vet. Res. , vol.64 , pp. 1088-1092
    • Chen, P.W.1    Shyu, C.L.2    Mao, F.C.3
  • 16
    • 0346034649 scopus 로고    scopus 로고
    • Tryptophan-rich antimicrobial peptides: Comparative properties and membrane interactions
    • Schibli, D. J., Epand, R. F., Vogel, H. J., and Epand, R. M. (2002) Tryptophan-rich antimicrobial peptides: comparative properties and membrane interactions Biochem. Cell Biol. 80, 667-677
    • (2002) Biochem. Cell Biol. , vol.80 , pp. 667-677
    • Schibli, D.J.1    Epand, R.F.2    Vogel, H.J.3    Epand, R.M.4
  • 17
    • 69249142709 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial, cytolytic, and cell-penetrating peptides: From kinetics to thermodynamics
    • Almeida, P. F. and Pokorny, A. (2009) Mechanisms of antimicrobial, cytolytic, and cell-penetrating peptides: from kinetics to thermodynamics Biochemistry 48, 8083-8093
    • (2009) Biochemistry , vol.48 , pp. 8083-8093
    • Almeida, P.F.1    Pokorny, A.2
  • 18
    • 0026638745 scopus 로고
    • Antitumor-activity of magainin analogs against human lung-cancer cell-lines
    • Ohsaki, Y., Gazdar, A. F., Chen, H. C., and Johnson, B. E. (1992) Antitumor-activity of magainin analogs against human lung-cancer cell-lines Cancer Res. 52, 3534-3538
    • (1992) Cancer Res. , vol.52 , pp. 3534-3538
    • Ohsaki, Y.1    Gazdar, A.F.2    Chen, H.C.3    Johnson, B.E.4
  • 19
    • 7044235790 scopus 로고    scopus 로고
    • Thermodynamics of lipid-peptide interactions
    • Seelig, J. (2004) Thermodynamics of lipid-peptide interactions Biochim. Biophys. Acta 1666, 40-50
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 40-50
    • Seelig, J.1
  • 20
    • 3142691160 scopus 로고    scopus 로고
    • Cyclization increases the antimicrobial activity and selectivity of arginine- and tryptophan-containing hexapeptides
    • Dathe, M., Nikolenko, H., Klose, J., and Bienert, M. (2004) Cyclization increases the antimicrobial activity and selectivity of arginine- and tryptophan-containing hexapeptides Biochemistry 43, 9140-9150
    • (2004) Biochemistry , vol.43 , pp. 9140-9150
    • Dathe, M.1    Nikolenko, H.2    Klose, J.3    Bienert, M.4
  • 21
    • 3843109179 scopus 로고    scopus 로고
    • Bulky nonproteinogenic amino acids permit the design of very small and effective cationic antibacterial peptides
    • Haug, B. E., Stensen, W., Stiberg, T., and Svendsen, J. S. (2004) Bulky nonproteinogenic amino acids permit the design of very small and effective cationic antibacterial peptides J. Med. Chem. 47, 4159-4162
    • (2004) J. Med. Chem. , vol.47 , pp. 4159-4162
    • Haug, B.E.1    Stensen, W.2    Stiberg, T.3    Svendsen, J.S.4
  • 22
    • 40549118540 scopus 로고    scopus 로고
    • Minimum requirements of hydrophobic and hydrophilic features in cationic peptide antibiotics (CPAs): Pharmacophore generation and validation with cationic steroid antibiotics (CSAs)
    • Sundriyal, S., Sharma, R. K., Jain, R., and Bharatam, P. V. (2008) Minimum requirements of hydrophobic and hydrophilic features in cationic peptide antibiotics (CPAs): pharmacophore generation and validation with cationic steroid antibiotics (CSAs) J. Mol. Model. 14, 265-278
    • (2008) J. Mol. Model. , vol.14 , pp. 265-278
    • Sundriyal, S.1    Sharma, R.K.2    Jain, R.3    Bharatam, P.V.4
  • 23
    • 33749012269 scopus 로고    scopus 로고
    • Peptide-membrane interactions and mechanisms of membrane destruction by amphipathic alpha-helical antimicrobial peptides
    • Sato, H. and Felix, J. B. (2006) Peptide-membrane interactions and mechanisms of membrane destruction by amphipathic alpha-helical antimicrobial peptides Biochim. Biophys. Acta 1758, 1245-1256
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1245-1256
    • Sato, H.1    Felix, J.B.2
  • 24
    • 0022389171 scopus 로고
    • Cholesterol and the cell membrane
    • Yeagle, P. L. (1985) Cholesterol and the cell membrane, Biochim. Biophys. Acta 822.
    • (1985) Biochim. Biophys. Acta , vol.822
    • Yeagle, P.L.1
  • 25
    • 0019304366 scopus 로고
    • Erythrocyte membrane cholesterol: An explanation of the aging effect on the rate of hemolysis
    • Araki, K. and Rifkind, J. M. (1980) Erythrocyte membrane cholesterol: An explanation of the aging effect on the rate of hemolysis. Life Sci. 26.
    • (1980) Life Sci. , pp. 26
    • Araki, K.1    Rifkind, J.M.2
  • 26
    • 33845373254 scopus 로고    scopus 로고
    • Anticancer α-helical peptides and structure/function relationships underpinning their interactions with tumor cell membranes
    • Sarah, R., Dennison, M. W., Harris, F., and Phoenix, D. A. (2006) Anticancer α-helical peptides and structure/function relationships underpinning their interactions with tumor cell membranes, Curr. Protein Pept. Sci. 7.
    • (2006) Curr. Protein Pept. Sci. , vol.7
    • Sarah, R.1    Dennison, M.W.2    Harris, F.3    Phoenix, D.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.