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Volumn 101, Issue 4, 2012, Pages 1508-1517

Lytic peptides with improved stability and selectivity designed for cancer treatment

Author keywords

Acid activation; Cancer; Formulation; Histidine rich peptides; Macromolecular drug delivery; Multi drug resistance; Peptide aggregates; PH; Solvation; Stability

Indexed keywords

LYTIC PEPTIDE; PEPTIDE; PEPTIDE DERIVATIVE; PTP 7; UNCLASSIFIED DRUG;

EID: 84857504892     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.23043     Document Type: Article
Times cited : (32)

References (29)
  • 2
    • 0033328139 scopus 로고    scopus 로고
    • The contribution of P-glycoprotein to pharmacokinetic drug-drug interactions
    • Yu DK. 1999. The contribution of P-glycoprotein to pharmacokinetic drug-drug interactions. J Clin Pharmacol 39:1203-1211.
    • (1999) J Clin Pharmacol , vol.39 , pp. 1203-1211
    • Yu, D.K.1
  • 3
    • 0029190287 scopus 로고
    • The role of the MDR protein in altered drug translocation across tumor cell membranes
    • Roepe PD. 1995. The role of the MDR protein in altered drug translocation across tumor cell membranes. Biochim Biophys Acta 1241:385-405.
    • (1995) Biochim Biophys Acta , vol.1241 , pp. 385-405
    • Roepe, P.D.1
  • 5
    • 0033028126 scopus 로고    scopus 로고
    • Structure-antibacterial, antitumor and hemolytic activity relationships of cecropin A-magainin 2 and cecropin A-melitin hybrid peptides
    • Shin SY, Kang JH, Hahm KS. 1999. Structure-antibacterial, antitumor and hemolytic activity relationships of cecropin A-magainin 2 and cecropin A-melitin hybrid peptides. J Pept Res 53:82-90.
    • (1999) J Pept Res , vol.53 , pp. 82-90
    • Shin, S.Y.1    Kang, J.H.2    Hahm, K.S.3
  • 6
    • 0033974530 scopus 로고    scopus 로고
    • Effects of the hinge region of cecropin A(1-8)-magainin 2(1-12), a synthetic antimicrobial peptide, on liposomes, bacterial and tumor cells
    • Shin SY, Kang JH, Jang SY, Kim Y, Kim KL, Hahm K. 2000. Effects of the hinge region of cecropin A(1-8)-magainin 2(1-12), a synthetic antimicrobial peptide, on liposomes, bacterial and tumor cells. Biochim Biophys Acta 1463:209-218.
    • (2000) Biochim Biophys Acta , vol.1463 , pp. 209-218
    • Shin, S.Y.1    Kang, J.H.2    Jang, S.Y.3    Kim, Y.4    Kim, K.L.5    Hahm, K.6
  • 8
    • 0036793131 scopus 로고    scopus 로고
    • Enhanced anti-tumor activity and selectivity of lactoferrin-derived peptides
    • Yang N, Steven W, Steven JS, Rekdal Q. 2002. Enhanced anti-tumor activity and selectivity of lactoferrin-derived peptides. J Pept Res 60:187-197.
    • (2002) J Pept Res , vol.60 , pp. 187-197
    • Yang, N.1    Steven, W.2    Steven, J.S.3    Rekdal, Q.4
  • 9
    • 0037643495 scopus 로고    scopus 로고
    • Targeted destruction of normal and cancer cells through lutropin/choriogonadotropin receptors using hecate-betaCG conjugate
    • Zaleska M, Bodek G, Jana B, Hansel W, Ziecik AJ. 2003. Targeted destruction of normal and cancer cells through lutropin/choriogonadotropin receptors using hecate-betaCG conjugate. Exp Clin Endocrinol Diabetes 111:146-153.
    • (2003) Exp Clin Endocrinol Diabetes , vol.111 , pp. 146-153
    • Zaleska, M.1    Bodek, G.2    Jana, B.3    Hansel, W.4    Ziecik, A.J.5
  • 10
    • 0037367239 scopus 로고    scopus 로고
    • Membrane disrupting lytic peptide conjugates destroy hormone dependent and independent breast cancer cells in vitro and in vivo
    • Leuschner C, Enright FM, Gawronska B, Hansel W. 2003. Membrane disrupting lytic peptide conjugates destroy hormone dependent and independent breast cancer cells in vitro and in vivo. Breast Cancer Res Treat 78:17-27.
    • (2003) Breast Cancer Res Treat , vol.78 , pp. 17-27
    • Leuschner, C.1    Enright, F.M.2    Gawronska, B.3    Hansel, W.4
  • 13
    • 70449645023 scopus 로고    scopus 로고
    • The pH sensitivity of histidine-containing lytic peptides
    • Tu Z, Young A, Murphy C, Liang JF. 2009. The pH sensitivity of histidine-containing lytic peptides. J Pept Sci 15:790-795.
    • (2009) J Pept Sci , vol.15 , pp. 790-795
    • Tu, Z.1    Young, A.2    Murphy, C.3    Liang, J.F.4
  • 14
    • 67650501109 scopus 로고    scopus 로고
    • Constructing bioactive peptides with pH-dependent activities
    • Tu Z, Volk M, Shah K, Clerkin K, Liang JF. 2009. Constructing bioactive peptides with pH-dependent activities. Peptides 30:1523-1528.
    • (2009) Peptides , vol.30 , pp. 1523-1528
    • Tu, Z.1    Volk, M.2    Shah, K.3    Clerkin, K.4    Liang, J.F.5
  • 15
    • 50349090857 scopus 로고    scopus 로고
    • PrP(106-126) does not interact with membranes under physiological conditions
    • Henriques ST, Pattenden LK, Aguilar MI, Castanho MARB. 2008. PrP(106-126) does not interact with membranes under physiological conditions. Biophys J 95:1877-1889.
    • (2008) Biophys J , vol.95 , pp. 1877-1889
    • Henriques, S.T.1    Pattenden, L.K.2    Aguilar, M.I.3    Castanho, M.A.R.B.4
  • 17
    • 23844434035 scopus 로고    scopus 로고
    • Aluminum-triggered structural modifications and aggregation of β-amyloids
    • Ricchelli F, Drago D, Filippi B, Tognon G, Zatta P. 2005. Aluminum-triggered structural modifications and aggregation of β-amyloids. Cell Mol Life Sci 62:1724-1733.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 1724-1733
    • Ricchelli, F.1    Drago, D.2    Filippi, B.3    Tognon, G.4    Zatta, P.5
  • 18
    • 70449518987 scopus 로고    scopus 로고
    • Binding modes of thioflavin-T to the single-layer beta-sheet of the peptide self-assembly mimics
    • Wu C, Biancalana M, Koide S, Shea JE. 2009. Binding modes of thioflavin-T to the single-layer beta-sheet of the peptide self-assembly mimics. J Mol Biol 394:627-633.
    • (2009) J Mol Biol , vol.394 , pp. 627-633
    • Wu, C.1    Biancalana, M.2    Koide, S.3    Shea, J.E.4
  • 19
    • 27744493759 scopus 로고    scopus 로고
    • Correlation between the activities of α-helical antimicrobial peptides and hydrophobicities represented as RP HPLC retention times
    • Kim S, Kim SS, Lee BJ. 2005. Correlation between the activities of α-helical antimicrobial peptides and hydrophobicities represented as RP HPLC retention times. Peptides 26:2050-2056.
    • (2005) Peptides , vol.26 , pp. 2050-2056
    • Kim, S.1    Kim, S.S.2    Lee, B.J.3
  • 20
    • 0141741478 scopus 로고    scopus 로고
    • In vitro activities of native and designed peptide antibioticsagainst drug sensitive and resistant tumor cell lines
    • Kim S, Kim SS, Bang YJ, Kim SJ, Lee BJ. 2003. In vitro activities of native and designed peptide antibioticsagainst drug sensitive and resistant tumor cell lines. Peptides 24:945-953.
    • (2003) Peptides , vol.24 , pp. 945-953
    • Kim, S.1    Kim, S.S.2    Bang, Y.J.3    Kim, S.J.4    Lee, B.J.5
  • 21
    • 0035208031 scopus 로고    scopus 로고
    • Status of methods for assessing bacterial cell surface charge properties based on zeta potential measurements
    • Wilson WW, Wade MM, Holman SC, Champlin FR. 2001. Status of methods for assessing bacterial cell surface charge properties based on zeta potential measurements. J Microbiol Meth 43:153-164.
    • (2001) J Microbiol Meth , vol.43 , pp. 153-164
    • Wilson, W.W.1    Wade, M.M.2    Holman, S.C.3    Champlin, F.R.4
  • 22
    • 0342378042 scopus 로고    scopus 로고
    • Interaction of Alzheimer betaamyloid peptide(1-40) with lipid membranes
    • Terzi E, Hölzemann G, Seelig J. 1997. Interaction of Alzheimer betaamyloid peptide(1-40) with lipid membranes. Biochem 38:14845-14852.
    • (1997) Biochem , vol.38 , pp. 14845-14852
    • Terzi, E.1    Hölzemann, G.2    Seelig, J.3
  • 23
    • 0037442740 scopus 로고    scopus 로고
    • The identification of hydrophobic sites on the surface of proteins using absorption difference spectroscopy of bromophenol blue
    • Bertsch M, Mayburd AL, Kassner RJ. 2003. The identification of hydrophobic sites on the surface of proteins using absorption difference spectroscopy of bromophenol blue. Anal Biochem 313:187-195.
    • (2003) Anal Biochem , vol.313 , pp. 187-195
    • Bertsch, M.1    Mayburd, A.L.2    Kassner, R.J.3
  • 24
    • 1842687009 scopus 로고    scopus 로고
    • Degradation, receptor binding, insulin secreting and antihyperglycaemic actions of palmitate-derivatised native and Ala8-substituted GLP-1 analogues
    • Green BD, Gault VA, Mooney MH, Irwin N, Harriott P, Greer B, Bailey CJ, O'Harte FP, Flatt PR. 2004. Degradation, receptor binding, insulin secreting and antihyperglycaemic actions of palmitate-derivatised native and Ala8-substituted GLP-1 analogues. Biol Chem 385:169-177.
    • (2004) Biol Chem , vol.385 , pp. 169-177
    • Green, B.D.1    Gault, V.A.2    Mooney, M.H.3    Irwin, N.4    Harriott, P.5    Greer, B.6    Bailey, C.J.7    O'Harte, F.P.8    Flatt, P.R.9
  • 27
    • 0042698340 scopus 로고    scopus 로고
    • Synthesis of polyethylene glycol (PEG) derivatives and PEGylated-peptide biopolymer conjugates
    • Li J, Kao WJ. 2003. Synthesis of polyethylene glycol (PEG) derivatives and PEGylated-peptide biopolymer conjugates. Biomacromolecules 4:1055-1067.
    • (2003) Biomacromolecules , vol.4 , pp. 1055-1067
    • Li, J.1    Kao, W.J.2
  • 28
    • 33644618361 scopus 로고    scopus 로고
    • Development of liposomal capreomycin sulfate formulations: Effects of formulation variables on peptide encapsulation
    • Ricci M, Giovagnoli S, Blasi P, Schoubben A, Perioli L, Rossi C. 2006. Development of liposomal capreomycin sulfate formulations: Effects of formulation variables on peptide encapsulation. Int J Pharm 311:172-181.
    • (2006) Int J Pharm , vol.311 , pp. 172-181
    • Ricci, M.1    Giovagnoli, S.2    Blasi, P.3    Schoubben, A.4    Perioli, L.5    Rossi, C.6
  • 29
    • 23944513080 scopus 로고    scopus 로고
    • Stability of insulin during the erosion of poly(lactic acid) and poly(lactic-co-glycolic acid) microspheres
    • Ibrahim MA, Ismail A, Fetouh MI, Gopferich A. 2008. Stability of insulin during the erosion of poly(lactic acid) and poly(lactic-co-glycolic acid) microspheres. J Control Release 106:241-252.
    • (2008) J Control Release , vol.106 , pp. 241-252
    • Ibrahim, M.A.1    Ismail, A.2    Fetouh, M.I.3    Gopferich, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.