메뉴 건너뛰기




Volumn 13, Issue 6, 2012, Pages 6849-6862

Role of helicity on the anticancer mechanism of action of cationic-helical peptides

Author keywords

Anticancer peptides; Helicity; Hydrophobicity; Mechanism of action; Specificity

Indexed keywords

ALPHA HELICAL PEPTIDE A12L; ALPHA HELICAL PEPTIDE A20L; AMINO ACID; DEXTRO AMINO ACID; PEPTIDE DERIVATIVE; UNCLASSIFIED DRUG; ANTIMICROBIAL CATIONIC PEPTIDE; ANTINEOPLASTIC AGENT; CATION; PEPTIDE;

EID: 84862489506     PISSN: None     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms13066849     Document Type: Article
Times cited : (48)

References (22)
  • 3
    • 38349009178 scopus 로고    scopus 로고
    • Studies on anticancer activities of antimicrobial peptides
    • Hoskin, D.W.; Ramamoorthy, A. Studies on anticancer activities of antimicrobial peptides. Biochim. Biophys. Acta 2008, 1778, 357-375.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 357-375
    • Hoskin, D.W.1    Ramamoorthy, A.2
  • 4
    • 45549098010 scopus 로고    scopus 로고
    • Current progress and future challenges in the biochemical diagnosis and treatment of pheochromocytomas and paragangliomas
    • Eisenhofer, G.; Siegert, G.; Kotzerke, J.; Bornstein, S.R.; Pacak, K. Current progress and future challenges in the biochemical diagnosis and treatment of pheochromocytomas and paragangliomas. Horm. Metab. Res. 2008, 40, 329-337.
    • (2008) Horm. Metab. Res , vol.40 , pp. 329-337
    • Eisenhofer, G.1    Siegert, G.2    Kotzerke, J.3    Bornstein, S.R.4    Pacak, K.5
  • 5
    • 33845373254 scopus 로고    scopus 로고
    • Anticancer alpha-helical peptides and structure/function relationships underpinning their interactions with tumour cell membranes
    • Dennison, S.R.; Whittaker, M.; Harris, F.; Phoenix, D.A. Anticancer alpha-helical peptides and structure/function relationships underpinning their interactions with tumour cell membranes. Curr. Protein Pept. Sci. 2006, 7, 487-499.
    • (2006) Curr. Protein Pept. Sci , vol.7 , pp. 487-499
    • Dennison, S.R.1    Whittaker, M.2    Harris, F.3    Phoenix, D.A.4
  • 6
    • 18544366816 scopus 로고    scopus 로고
    • Host defense peptides as new weapons in cancer treatment
    • Papo, N.; Shai, Y. Host defense peptides as new weapons in cancer treatment. Cell Mol. Life Sci. 2005, 62, 784-790.
    • (2005) Cell Mol. Life Sci , vol.62 , pp. 784-790
    • Papo, N.1    Shai, Y.2
  • 7
    • 0036829110 scopus 로고    scopus 로고
    • Increased exposure of anionic phospholipids on the surface of tumor blood vessels
    • Ran, S.; Downes, A.; Thorpe, P.E. Increased exposure of anionic phospholipids on the surface of tumor blood vessels. Cancer Res. 2002, 62, 6132-6140.
    • (2002) Cancer Res , vol.62 , pp. 6132-6140
    • Ran, S.1    Downes, A.2    Thorpe, P.E.3
  • 8
    • 0029930750 scopus 로고    scopus 로고
    • Effect of O-glycosylated mucin on invasion and metastasis of HM7 human colon cancer cells
    • Yoon, W.H.; Park, H.D.; Lim, K.; Hwang, B.D. Effect of O-glycosylated mucin on invasion and metastasis of HM7 human colon cancer cells. Biochem. Biophys. Res. Commun. 1996, 222, 694-699.
    • (1996) Biochem. Biophys. Res. Commun , vol.222 , pp. 694-699
    • Yoon, W.H.1    Park, H.D.2    Lim, K.3    Hwang, B.D.4
  • 9
    • 0032938321 scopus 로고    scopus 로고
    • Membrane fluidity characteristics of human lung cancer
    • Sok, M.; Sentjurc, M.; Schara, M. Membrane fluidity characteristics of human lung cancer. Cancer Lett. 1999, 139, 215-220.
    • (1999) Cancer Lett , vol.139 , pp. 215-220
    • Sok, M.1    Sentjurc, M.2    Schara, M.3
  • 10
    • 0029031058 scopus 로고
    • Scanning electron microscopic analysis of breast aspirates
    • Chaudhary, J.; Munshi, M. Scanning electron microscopic analysis of breast aspirates. Cytopathology 1995, 6, 162-167.
    • (1995) Cytopathology , vol.6 , pp. 162-167
    • Chaudhary, J.1    Munshi, M.2
  • 11
    • 79955748813 scopus 로고    scopus 로고
    • Studies on mechanism of action of anticancer peptides by modulation of hydrophobicity within a defined structural framework
    • Huang, Y.B.; Wang, X.F.; Wang, H.Y.; Liu, Y.; Chen, Y. Studies on mechanism of action of anticancer peptides by modulation of hydrophobicity within a defined structural framework. Mol. Cancer Ther. 2011, 10, 416-426.
    • (2011) Mol. Cancer Ther , vol.10 , pp. 416-426
    • Huang, Y.B.1    Wang, X.F.2    Wang, H.Y.3    Liu, Y.4    Chen, Y.5
  • 12
    • 16844373772 scopus 로고    scopus 로고
    • Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index
    • Chen, Y.; Mant, C.T.; Farmer, S.W.; Hancock, R.E.; Vasil, M.L.; Hodges, R.S. Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index. J. Biol. Chem. 2005, 280, 12316-12329.
    • (2005) J. Biol. Chem , vol.280 , pp. 12316-12329
    • Chen, Y.1    Mant, C.T.2    Farmer, S.W.3    Hancock, R.E.4    Vasil, M.L.5    Hodges, R.S.6
  • 13
    • 0036185353 scopus 로고    scopus 로고
    • Determination of stereochemistry stability coefficients of amino acid side-chains in an amphipathic alpha-helix
    • Chen, Y.; Mant, C.T.; Hodges, R.S. Determination of stereochemistry stability coefficients of amino acid side-chains in an amphipathic alpha-helix. J. Pept. Res. 2002, 59, 18-33.
    • (2002) J. Pept. Res , vol.59 , pp. 18-33
    • Chen, Y.1    Mant, C.T.2    Hodges, R.S.3
  • 14
    • 0024982236 scopus 로고
    • Effect of preferred binding domains on peptide retention behavior in reversed-phase chromatography
    • Zhou, N.E.; Mant, C.T.; Hodges, R.S. Effect of preferred binding domains on peptide retention behavior in reversed-phase chromatography: Amphipathic alpha-helices. Pept. Res. 1990, 3, 8-20.
    • (1990) Amphipathic Alpha-helices. Pept. Res , vol.3 , pp. 8-20
    • Zhou, N.E.1    Mant, C.T.2    Hodges, R.S.3
  • 15
    • 33646231485 scopus 로고    scopus 로고
    • Determination of intrinsic hydrophilicity/hydrophobicity of amino acid side chains in peptides in the absence of nearest-neighbor or conformational effects
    • Kovacs, J.M.; Mant, C.T.; Hodges, R.S. Determination of intrinsic hydrophilicity/hydrophobicity of amino acid side chains in peptides in the absence of nearest-neighbor or conformational effects. Biopolymers 2006, 84, 283-297.
    • (2006) Biopolymers , vol.84 , pp. 283-297
    • Kovacs, J.M.1    Mant, C.T.2    Hodges, R.S.3
  • 17
    • 0031005930 scopus 로고    scopus 로고
    • A repertoire of novel antibacterial diastereomeric peptides with selective cytolytic activity
    • Oren, Z.; Hong, J.; Shai, Y. A repertoire of novel antibacterial diastereomeric peptides with selective cytolytic activity. J. Biol. Chem. 1997, 272, 14643-14649.
    • (1997) J. Biol. Chem , vol.272 , pp. 14643-14649
    • Oren, Z.1    Hong, J.2    Shai, Y.3
  • 18
    • 0042573730 scopus 로고    scopus 로고
    • New lytic peptides based on the D,L-amphipathic helix motif preferentially kill tumor cells compared to normal cells
    • Papo, N.; Shai, Y. New lytic peptides based on the D,L-amphipathic helix motif preferentially kill tumor cells compared to normal cells. Biochemistry 2003, 42, 9346-9354.
    • (2003) Biochemistry , vol.42 , pp. 9346-9354
    • Papo, N.1    Shai, Y.2
  • 19
    • 0037742621 scopus 로고    scopus 로고
    • A novel lytic peptide composed of DL-amino acids selectively kills cancer cells in culture and in mice
    • Papo, N.; Shahar, M.; Eisenbach, L.; Shai, Y. A novel lytic peptide composed of DL-amino acids selectively kills cancer cells in culture and in mice. J. Biol. Chem. 2003, 278, 21018-21023.
    • (2003) J. Biol. Chem , vol.278 , pp. 21018-21023
    • Papo, N.1    Shahar, M.2    Eisenbach, L.3    Shai, Y.4
  • 20
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Shai, Y. Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides. Biochim. Biophys. Acta 1999, 1462, 55-70.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 22
    • 76049129382 scopus 로고    scopus 로고
    • Structure-guided de novo design of α-helical antimicrobial peptide with enhanced specificity
    • Huang, J.F.; Xu, Y.M.; Hao, D.M.; Huang, Y.B.; Liu, Y.; Chen, Y.X. Structure-guided de novo design of α-helical antimicrobial peptide with enhanced specificity. Pure Appl. Chem. 2010, 82, 243-257.
    • (2010) Pure Appl. Chem , vol.82 , pp. 243-257
    • Huang, J.F.1    Xu, Y.M.2    Hao, D.M.3    Huang, Y.B.4    Liu, Y.5    Chen, Y.X.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.