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Volumn 57, Issue 7, 2014, Pages 2864-2873

Tailoring cytotoxicity of antimicrobial peptidomimetics with high activity against multidrug-resistant Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

CEFOTAXIME; GENTAMICIN; OLIGOMER; PEPTIDOMIMETIC AGENT; PEPTOID; VANCOMYCIN;

EID: 84898432553     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm401335p     Document Type: Article
Times cited : (44)

References (37)
  • 1
    • 77951132271 scopus 로고    scopus 로고
    • ECDC/EMEA Joint Technical Report; European Centre for Disease Prevention and Control and European Medicines Agency: Stockholm, Sweden.
    • The Bacterial Challenge: Time To React; ECDC/EMEA Joint Technical Report; European Centre for Disease Prevention and Control and European Medicines Agency: Stockholm, Sweden, 2009.
    • (2009) The Bacterial Challenge: Time to React
  • 4
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff, M. Antimicrobial peptides of multicellular organisms Nature 2002, 415, 389-395
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 5
    • 33845699790 scopus 로고    scopus 로고
    • Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies
    • Hancock, R. E. W.; Sahl, H. G. Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies Nat. Biotechnol. 2006, 24, 1551-1557
    • (2006) Nat. Biotechnol. , vol.24 , pp. 1551-1557
    • Hancock, R.E.W.1    Sahl, H.G.2
  • 6
    • 77958178550 scopus 로고    scopus 로고
    • Optimised therapeutic peptides - From sequence to drug
    • Haberl, U.; Rybka, A.; Frank, H. Optimised therapeutic peptides - from sequence to drug Eur. Biopharm. Rev. 2009, 32-40
    • (2009) Eur. Biopharm. Rev. , pp. 32-40
    • Haberl, U.1    Rybka, A.2    Frank, H.3
  • 7
    • 65949101647 scopus 로고    scopus 로고
    • Advances in peptide pharmaceuticals
    • Stevenson, C. L. Advances in peptide pharmaceuticals Curr. Pharm. Biotechnol. 2009, 10, 122-137
    • (2009) Curr. Pharm. Biotechnol. , vol.10 , pp. 122-137
    • Stevenson, C.L.1
  • 9
    • 77950241221 scopus 로고    scopus 로고
    • Emerging peptide therapeutics for inflammatory autoimmune diseases
    • Briand, J. P.; Muller, S. Emerging peptide therapeutics for inflammatory autoimmune diseases Curr. Pharm. Des. 2010, 16, 1136-1142
    • (2010) Curr. Pharm. Des. , vol.16 , pp. 1136-1142
    • Briand, J.P.1    Muller, S.2
  • 10
    • 79251521467 scopus 로고    scopus 로고
    • Clinical development of peptide antibiotics
    • Jenssen, H. Clinical development of peptide antibiotics Pharma Chem. 2009, 8, 22-26
    • (2009) Pharma Chem. , vol.8 , pp. 22-26
    • Jenssen, H.1
  • 11
    • 84934444542 scopus 로고    scopus 로고
    • Peptide-based drug design: Here and now
    • Otvos, L., Jr. Peptide-based drug design: here and now Methods Mol. Biol. 2008, 494, 1-8
    • (2008) Methods Mol. Biol. , vol.494 , pp. 1-8
    • Otvos Jr., L.1
  • 12
    • 84866943640 scopus 로고    scopus 로고
    • Antimicrobial activity of peptidomimetics against multidrug-resistant Escherichia coli: A comparative study of different backbones
    • Jahnsen, R. D.; Frimodt-Møller, N.; Franzyk, H. Antimicrobial activity of peptidomimetics against multidrug-resistant Escherichia coli: a comparative study of different backbones J. Med. Chem. 2012, 55, 7253-7261
    • (2012) J. Med. Chem. , vol.55 , pp. 7253-7261
    • Jahnsen, R.D.1    Frimodt-Møller, N.2    Franzyk, H.3
  • 13
    • 77954373564 scopus 로고    scopus 로고
    • Antimicrobial, hemolytic, and cytotoxic activities of β-peptoid-peptide hybrid oligomers: Improved properties compared to natural AMPs
    • Olsen, C. A.; Ziegler, H. L.; Nielsen, H. M.; Frimodt-Møller, N.; Jaroszewski, J. W.; Franzyk, H. Antimicrobial, hemolytic, and cytotoxic activities of β-peptoid-peptide hybrid oligomers: improved properties compared to natural AMPs ChemBioChem 2010, 11, 1356-1360
    • (2010) ChemBioChem , vol.11 , pp. 1356-1360
    • Olsen, C.A.1    Ziegler, H.L.2    Nielsen, H.M.3    Frimodt-Møller, N.4    Jaroszewski, J.W.5    Franzyk, H.6
  • 15
    • 49649115502 scopus 로고    scopus 로고
    • Dimeric building blocks for solid-phase synthesis of α-peptide- β-peptoid chimeras
    • Bonke, G.; Vedel, L.; Witt, M.; Jaroszewski, J. W.; Olsen, C. A.; Franzyk, H. Dimeric building blocks for solid-phase synthesis of α-peptide-β-peptoid chimeras Synthesis 2008, 2381-2390
    • (2008) Synthesis , pp. 2381-2390
    • Bonke, G.1    Vedel, L.2    Witt, M.3    Jaroszewski, J.W.4    Olsen, C.A.5    Franzyk, H.6
  • 16
    • 33750060074 scopus 로고    scopus 로고
    • Synthesis and circular dichroism spectroscopic investigations of oligomeric β-peptoids with α-chiral side chains
    • Norgren, A. S.; Zhang, S.; Arvidsson, P. I. Synthesis and circular dichroism spectroscopic investigations of oligomeric β-peptoids with α-chiral side chains Org. Lett. 2006, 8, 4533-4536
    • (2006) Org. Lett. , vol.8 , pp. 4533-4536
    • Norgren, A.S.1    Zhang, S.2    Arvidsson, P.I.3
  • 17
    • 0031875776 scopus 로고    scopus 로고
    • Solid-phase syntheses of peptoids using Fmoc-protected N-substituted glycines: The synthesis of (retro) peptoids of Leu-enkephalin and substance P
    • Kruijtzer, J. A. W.; Hofmeyer, L. J. F.; Heerma, W.; Versluis, C.; Liskamp, R. M. J. Solid-phase syntheses of peptoids using Fmoc-protected N-substituted glycines: the synthesis of (retro) peptoids of Leu-enkephalin and substance P Chem. - Eur. J. 1998, 4, 1570-1580
    • (1998) Chem. - Eur. J. , vol.4 , pp. 1570-1580
    • Kruijtzer, J.A.W.1    Hofmeyer, L.J.F.2    Heerma, W.3    Versluis, C.4    Liskamp, R.M.J.5
  • 19
    • 0025899234 scopus 로고
    • Use of an aqueous soluble tetrazolium formazan assay for cell-growth assays in culture
    • Cory, A. H.; Owen, T. C.; Barltrop, J. A.; Cory, J. G. Use of an aqueous soluble tetrazolium formazan assay for cell-growth assays in culture Cancer Commun. 1991, 3, 207-212
    • (1991) Cancer Commun. , vol.3 , pp. 207-212
    • Cory, A.H.1    Owen, T.C.2    Barltrop, J.A.3    Cory, J.G.4
  • 21
    • 84864065351 scopus 로고    scopus 로고
    • Membrane adsorption and binding, cellular uptake and cytotoxicity of cell-penetrating peptidomimetics with α-peptide/β-peptoid backbone: Effects of hydrogen bonding and α-chirality in the β-peptoid residues
    • Jing, X.; Yang, M.; Kasimova, M. R.; Malmsten, M.; Franzyk, H.; Jorgensen, L.; Foged, C.; Nielsen, H. M. Membrane adsorption and binding, cellular uptake and cytotoxicity of cell-penetrating peptidomimetics with α-peptide/β-peptoid backbone: effects of hydrogen bonding and α-chirality in the β-peptoid residues Biochem. Biophys. Acta 2012, 1818, 2660-2668
    • (2012) Biochem. Biophys. Acta , vol.1818 , pp. 2660-2668
    • Jing, X.1    Yang, M.2    Kasimova, M.R.3    Malmsten, M.4    Franzyk, H.5    Jorgensen, L.6    Foged, C.7    Nielsen, H.M.8
  • 22
    • 16844373772 scopus 로고    scopus 로고
    • Rational design of α-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index
    • Chen, Y. X.; Mant, C. T.; Farmer, S. W.; Hancock, R. E. W.; Vasil, M. L.; Hodges, R. S. Rational design of α-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.X.1    Mant, C.T.2    Farmer, S.W.3    Hancock, R.E.W.4    Vasil, M.L.5    Hodges, R.S.6
  • 23
    • 77249095412 scopus 로고    scopus 로고
    • Antimicrobial activity of small β-peptidomimetics based on the pharmacophore model of short cationic antimicrobial peptides
    • Hansen, T.; Alst, T.; Havelkova, M.; Strøm, M. B. Antimicrobial activity of small β-peptidomimetics based on the pharmacophore model of short cationic antimicrobial peptides J. Med. Chem. 2009, 53, 595-606
    • (2009) J. Med. Chem. , vol.53 , pp. 595-606
    • Hansen, T.1    Alst, T.2    Havelkova, M.3    Strøm, M.B.4
  • 24
    • 34249070808 scopus 로고    scopus 로고
    • Substitution of the leucine zipper sequence in melittin with peptoid residues affects self-association, cell selectivity, and mode of action
    • Zhu, W. L.; Song, Y. M.; Park, Y.; Park, K. H.; Yang, S. T.; Kim, J. I.; Park, I. S.; Hahm, K. S.; Shin, S. Y. Substitution of the leucine zipper sequence in melittin with peptoid residues affects self-association, cell selectivity, and mode of action Biochem. Biophys. Acta 2007, 1768, 1506-1517
    • (2007) Biochem. Biophys. Acta , vol.1768 , pp. 1506-1517
    • Zhu, W.L.1    Song, Y.M.2    Park, Y.3    Park, K.H.4    Yang, S.T.5    Kim, J.I.6    Park, I.S.7    Hahm, K.S.8    Shin, S.Y.9
  • 25
    • 38349009178 scopus 로고    scopus 로고
    • Studies on anticancer activities of antimicrobial peptides
    • Hoskin, D. W.; Ramamoorthy, A. Studies on anticancer activities of antimicrobial peptides Biochem. Biophys. Acta 2008, 1778, 357-375
    • (2008) Biochem. Biophys. Acta , vol.1778 , pp. 357-375
    • Hoskin, D.W.1    Ramamoorthy, A.2
  • 26
    • 84858381864 scopus 로고    scopus 로고
    • Modulating immunity as a therapy for bacterial infections
    • Hancock, R. E. W.; Nijnik, A.; Philpott, D. J. Modulating immunity as a therapy for bacterial infections Nat. Rev. Microbiol. 2012, 10, 243-254
    • (2012) Nat. Rev. Microbiol. , vol.10 , pp. 243-254
    • Hancock, R.E.W.1    Nijnik, A.2    Philpott, D.J.3
  • 28
    • 33846922033 scopus 로고    scopus 로고
    • Assessing the data quality in predictive toxicology using a panel of cell lines and cytotoxicity assays
    • Pohjala, L.; Tammela, P.; Samanta, S. K.; Yli-Kauhaluoma, J.; Vuorela, P. Assessing the data quality in predictive toxicology using a panel of cell lines and cytotoxicity assays Anal. Biochem. 2007, 362, 221-228
    • (2007) Anal. Biochem. , vol.362 , pp. 221-228
    • Pohjala, L.1    Tammela, P.2    Samanta, S.K.3    Yli-Kauhaluoma, J.4    Vuorela, P.5
  • 29
    • 3142646879 scopus 로고    scopus 로고
    • Evaluation of different toxicity assays applied to proliferating cells and to stratified epithelium in relation to permeability enhancement with glycocholate
    • Eirheim, H. U.; Bundgaard, C.; Nielsen, H. M. Evaluation of different toxicity assays applied to proliferating cells and to stratified epithelium in relation to permeability enhancement with glycocholate Toxicol. in Vitro 2004, 18, 649-657
    • (2004) Toxicol. in Vitro , vol.18 , pp. 649-657
    • Eirheim, H.U.1    Bundgaard, C.2    Nielsen, H.M.3
  • 30
    • 0034835809 scopus 로고    scopus 로고
    • Peptoid oligomers with α-chiral, aromatic side chains: Sequence requirements for the formation of stable peptoid helices
    • Wu, C. W.; Sanborn, T. J.; Huang, K.; Zuckermann, R. N.; Barron, A. E. Peptoid oligomers with α-chiral, aromatic side chains: sequence requirements for the formation of stable peptoid helices J. Am. Chem. Soc. 2001, 123, 6778-6784
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 6778-6784
    • Wu, C.W.1    Sanborn, T.J.2    Huang, K.3    Zuckermann, R.N.4    Barron, A.E.5
  • 32
    • 79959367332 scopus 로고    scopus 로고
    • Bacterial membrane activity of α-peptide/β-peptoid chimeras: Influence of amino acid composition and chain length on the activity against different bacterial strains
    • Hein-Kristensen, L.; Knapp, K.; Franzyk, H.; Gram, L. Bacterial membrane activity of α-peptide/β-peptoid chimeras: influence of amino acid composition and chain length on the activity against different bacterial strains BMC Microbiol. 2011, 11, 144
    • (2011) BMC Microbiol. , vol.11 , pp. 144
    • Hein-Kristensen, L.1    Knapp, K.2    Franzyk, H.3    Gram, L.4
  • 33
    • 33846251959 scopus 로고    scopus 로고
    • Interplay among folding, sequence, and lipophilicity in the antibacterial and hemolytic activities of α/β-peptides
    • Schmitt, M. A.; Weisblum, B.; Gellman, S. H. Interplay among folding, sequence, and lipophilicity in the antibacterial and hemolytic activities of α/β-peptides J. Am. Chem. Soc. 2007, 129, 417-428
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 417-428
    • Schmitt, M.A.1    Weisblum, B.2    Gellman, S.H.3
  • 35
    • 0021909644 scopus 로고
    • Production of large unilamellar vesicles by a rapid extrusion procedure - Characterization of size distribution, trapped volume and ability to maintain a membrane-potential
    • Hope, M. J.; Bally, M. B.; Webb, G.; Cullis, P. R. Production of large unilamellar vesicles by a rapid extrusion procedure - characterization of size distribution, trapped volume and ability to maintain a membrane-potential Biochim. Biophys. Acta 1985, 812, 55-65
    • (1985) Biochim. Biophys. Acta , vol.812 , pp. 55-65
    • Hope, M.J.1    Bally, M.B.2    Webb, G.3    Cullis, P.R.4
  • 36
    • 77958124580 scopus 로고    scopus 로고
    • Dual functions of the human antimicrobial peptide LL-37 - Target membrane perturbation and host cell cargo delivery
    • Zhang, X. A.; Oglecka, K.; Sandgren, S.; Belting, M.; Esbjorner, E. K.; Norden, B.; Graslund, A. Dual functions of the human antimicrobial peptide LL-37 - target membrane perturbation and host cell cargo delivery Biochem. Biophys. Acta 2010, 1798, 2201-2208
    • (2010) Biochem. Biophys. Acta , vol.1798 , pp. 2201-2208
    • Zhang, X.A.1    Oglecka, K.2    Sandgren, S.3    Belting, M.4    Esbjorner, E.K.5    Norden, B.6    Graslund, A.7
  • 37
    • 34548847733 scopus 로고    scopus 로고
    • Using circular dichroism spectra to estimate protein secondary structure
    • Greenfield, N. J. Using circular dichroism spectra to estimate protein secondary structure Nat. Protoc. 2006, 1, 2876-2890
    • (2006) Nat. Protoc. , vol.1 , pp. 2876-2890
    • Greenfield, N.J.1


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