메뉴 건너뛰기




Volumn 1798, Issue 10, 2010, Pages 1864-1875

Interaction studies of novel cell selective antimicrobial peptides with model membranes and E. coli ATCC 11775

Author keywords

Amphipathic; Antimicrobial peptides; Hemolytic activity; Membrane active; Microscopy

Indexed keywords

AMIKACIN; ANTIMICROBIAL PEPTIDE SA 1; ANTIMICROBIAL PEPTIDE SA 2; ANTIMICROBIAL PEPTIDE SA 3; ANTIMICROBIAL PEPTIDE SA 4; ANTIMICROBIAL PEPTIDE SA 5; ANTIMICROBIAL PEPTIDE SA 6; CALCEIN; CEFOPERAZONE; CEFOTAXIME; CIPROFLOXACIN; IMIPENEM; INDOLICIDIN; NETILMICIN; PIPERACILLIN; PIPERACILLIN PLUS TAZOBACTAM; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG; ANTIINFECTIVE AGENT; ANTIMICROBIAL CATIONIC PEPTIDE; LIPID BILAYER; PEPTIDE; PROTEIN BINDING;

EID: 77955657627     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2010.06.016     Document Type: Article
Times cited : (74)

References (49)
  • 1
    • 0037439518 scopus 로고    scopus 로고
    • Bacterial resistance: origin, epidemiology and impact
    • Livermore D.M. Bacterial resistance: origin, epidemiology and impact. Clin. Infect. Dis. 2003, 36:11-23.
    • (2003) Clin. Infect. Dis. , vol.36 , pp. 11-23
    • Livermore, D.M.1
  • 2
    • 34548021916 scopus 로고    scopus 로고
    • Resistance to antibiotics
    • Sanchez J.S. Resistance to antibiotics. J. Bacteriol. 2006, 48:105-112.
    • (2006) J. Bacteriol. , vol.48 , pp. 105-112
    • Sanchez, J.S.1
  • 4
    • 36749025072 scopus 로고    scopus 로고
    • Bad bugs need more drugs
    • Opar A. Bad bugs need more drugs. Nat. Rev. Drug Discov. 2007, 6:943-944.
    • (2007) Nat. Rev. Drug Discov. , vol.6 , pp. 943-944
    • Opar, A.1
  • 5
    • 12944302098 scopus 로고    scopus 로고
    • Lack of development of new antimicrobial drugs: a potential serious threat to public health
    • Norrby S.R., Nord C.E., Finch R. Lack of development of new antimicrobial drugs: a potential serious threat to public health. Lancet Infect. Dis. 2005, 5:115-119.
    • (2005) Lancet Infect. Dis. , vol.5 , pp. 115-119
    • Norrby, S.R.1    Nord, C.E.2    Finch, R.3
  • 6
    • 61349169039 scopus 로고    scopus 로고
    • Up immunity: how antimicrobial peptides have multiple roles in immune defense
    • Lai Y., Gallo AMPed R.L. up immunity: how antimicrobial peptides have multiple roles in immune defense. Trends Immunol. 2009, 3:131-141.
    • (2009) Trends Immunol. , vol.3 , pp. 131-141
    • Lai, Y.1    Gallo AMPed, R.L.2
  • 7
    • 0034255255 scopus 로고    scopus 로고
    • The role of antimicrobial peptides in animal defenses
    • Hancock R.E.W., Scott M.G. The role of antimicrobial peptides in animal defenses. Proc. Natl Acad. Sci. U. S. A. 2000, 97:8856-8861.
    • (2000) Proc. Natl Acad. Sci. U. S. A. , vol.97 , pp. 8856-8861
    • Hancock, R.E.W.1    Scott, M.G.2
  • 8
    • 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
  • 10
    • 0032717048 scopus 로고    scopus 로고
    • Diversity of antimicrobial peptides and their mechanisms of action
    • Epand R.M., Vogel H.J. Diversity of antimicrobial peptides and their mechanisms of action. Biochim. Biophys. Acta 1999, 1462:11-28.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 11-28
    • Epand, R.M.1    Vogel, H.J.2
  • 11
    • 0035719931 scopus 로고    scopus 로고
    • Amphipathic α helical antimicrobial peptides
    • Giangaspero A., Sandri L., Tossi A. Amphipathic α helical antimicrobial peptides. Eur. J. Biochem. 2001, 268:5589-5600.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5589-5600
    • Giangaspero, A.1    Sandri, L.2    Tossi, A.3
  • 12
    • 26644469527 scopus 로고    scopus 로고
    • Basis for selectivity of cationic antimicrobial peptides for bacterial versus mammalian membranes
    • Glukhov E., Stark M., Burrows L.L., Deber C.M. Basis for selectivity of cationic antimicrobial peptides for bacterial versus mammalian membranes. J. Biol. Chem. 2005, 280:33960-33967.
    • (2005) J. Biol. Chem. , vol.280 , pp. 33960-33967
    • Glukhov, E.1    Stark, M.2    Burrows, L.L.3    Deber, C.M.4
  • 13
    • 65249175757 scopus 로고    scopus 로고
    • Cell specificity, anti-inflammatory activity, and plausible bactericidal mechanism of designed Trp-rich model antimicrobial peptides
    • Park K.H., Nan Y.H., Park Y., Kim J.I., Park I.S., Hahm K.S., Shin S.Y. Cell specificity, anti-inflammatory activity, and plausible bactericidal mechanism of designed Trp-rich model antimicrobial peptides. Biochim. Biophys. Acta 2009, 1788:1193-1203.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1193-1203
    • Park, K.H.1    Nan, Y.H.2    Park, Y.3    Kim, J.I.4    Park, I.S.5    Hahm, K.S.6    Shin, S.Y.7
  • 14
    • 33748933561 scopus 로고    scopus 로고
    • Alpha-helical antimicrobial peptides-Using a sequence template to guide structure activity relationship studies
    • Zelezetsky I., Tossi A. Alpha-helical antimicrobial peptides-Using a sequence template to guide structure activity relationship studies. Biochim. Biophys. Acta 2006, 1758:1436-1449.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1436-1449
    • Zelezetsky, I.1    Tossi, A.2
  • 15
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?
    • Brogden K.A. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?. Nat. Rev. Microbiol. 2005, 3:238-250.
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 16
    • 0036214967 scopus 로고    scopus 로고
    • Intracellular targets of antibacterial peptides
    • Cudic M., Otvos L. Intracellular targets of antibacterial peptides. Curr. Drug Targets 2002, 3:101-106.
    • (2002) Curr. Drug Targets , vol.3 , pp. 101-106
    • Cudic, M.1    Otvos, L.2
  • 17
    • 0042905861 scopus 로고    scopus 로고
    • The role of antimicrobial peptides in innate immunity
    • Ganz T. The role of antimicrobial peptides in innate immunity. Integr. Comp. Biol. 2003, 43:300-304.
    • (2003) Integr. Comp. Biol. , vol.43 , pp. 300-304
    • Ganz, T.1
  • 18
    • 65949090768 scopus 로고    scopus 로고
    • Domains in bacterial membranes and the action of antimicrobial agents
    • Epand R.M., Epand R.F. Domains in bacterial membranes and the action of antimicrobial agents. Mol. Biosyst. 2009, 5:580-587.
    • (2009) Mol. Biosyst. , vol.5 , pp. 580-587
    • Epand, R.M.1    Epand, R.F.2
  • 19
    • 0022699646 scopus 로고
    • Solid phase synthesis
    • Merrifield R.B. Solid phase synthesis. Science 1986, 232:341-347.
    • (1986) Science , vol.232 , pp. 341-347
    • Merrifield, R.B.1
  • 20
    • 0001439249 scopus 로고    scopus 로고
    • Structure-activity analysis of buforin II, a histone H2A-derived antimicrobial peptide: The Proline hinge is responsible for the cell-penetrating ability of buforin II
    • Chan B.P., Kwan S.Y., Matsuzaki K., Kim M.S., Kim S.C. Structure-activity analysis of buforin II, a histone H2A-derived antimicrobial peptide: The Proline hinge is responsible for the cell-penetrating ability of buforin II. Proc. Natl. Acad. Sci. U. S. A. 2000, 97:8245-8250.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 8245-8250
    • Chan, B.P.1    Kwan, S.Y.2    Matsuzaki, K.3    Kim, M.S.4    Kim, S.C.5
  • 22
    • 33750080503 scopus 로고    scopus 로고
    • De novo designed cyclic cationic peptides as inhibitors of plant pathogenic bacteria
    • Monroc S., Badosa E., Feliu L., Planas M., Montesinos E., Bardaji E. De novo designed cyclic cationic peptides as inhibitors of plant pathogenic bacteria. Peptides 2006, 27:2567-2574.
    • (2006) Peptides , vol.27 , pp. 2567-2574
    • Monroc, S.1    Badosa, E.2    Feliu, L.3    Planas, M.4    Montesinos, E.5    Bardaji, E.6
  • 23
    • 0021755639 scopus 로고
    • Differential light scattering and absorption flattening optical effects are minimal in the circular dichroism spectra of small unilamellar vesicles
    • Mao D., Wallace B.A. Differential light scattering and absorption flattening optical effects are minimal in the circular dichroism spectra of small unilamellar vesicles. Biochemistry 1984, 23:2667-2673.
    • (1984) Biochemistry , vol.23 , pp. 2667-2673
    • Mao, D.1    Wallace, B.A.2
  • 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., Park 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. Biochim. Biophys. Acta 2007, 1768:1506-1517.
    • (2007) Biochim. 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.6    Park, S.7    Hahm, K.S.8    Shin, S.Y.9
  • 25
    • 0035929565 scopus 로고    scopus 로고
    • Interaction of cationic antimicrobial peptides with model membranes
    • Zhang L., Rozek A., Hancock R.E.W. Interaction of cationic antimicrobial peptides with model membranes. J. Biol. Chem. 2001, 276:35714-35722.
    • (2001) J. Biol. Chem. , vol.276 , pp. 35714-35722
    • Zhang, L.1    Rozek, A.2    Hancock, R.E.W.3
  • 26
    • 70449246528 scopus 로고
    • Phosphorus assay in column chromatography
    • Bartlett G.R. Phosphorus assay in column chromatography. J. Biol. Chem. 1959, 234:466-468.
    • (1959) J. Biol. Chem. , vol.234 , pp. 466-468
    • Bartlett, G.R.1
  • 27
    • 33748988741 scopus 로고    scopus 로고
    • Tryptophan- and arginine-rich antimicrobial peptides: structures and mechanisms of action
    • Chan D.I., Prenner E.J., Vogel H.J. Tryptophan- and arginine-rich antimicrobial peptides: structures and mechanisms of action. Biochim. Biophys. Acta 2006, 1758:1184-1202.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1184-1202
    • Chan, D.I.1    Prenner, E.J.2    Vogel, H.J.3
  • 28
    • 0015522150 scopus 로고
    • Determination of secondary structure of proteins by circular dichroism and optical rotator dispersion
    • Chen Y.H., Yang J.T., Martinez H.M. Determination of secondary structure of proteins by circular dichroism and optical rotator dispersion. Biochemistry 1972, 11:4120-4123.
    • (1972) Biochemistry , vol.11 , pp. 4120-4123
    • Chen, Y.H.1    Yang, J.T.2    Martinez, H.M.3
  • 29
    • 0037184029 scopus 로고    scopus 로고
    • NMR Structure of PW2 bound to SDS micelles: a tryptophan-rich anticoccidial peptide selected from phage display libraries
    • Tinoco L.W., da Silva A., Leite A., Valente A.P., Almeida F.C.L. NMR Structure of PW2 bound to SDS micelles: a tryptophan-rich anticoccidial peptide selected from phage display libraries. J. Biol. Chem. 2002, 277:36351-36356.
    • (2002) J. Biol. Chem. , vol.277 , pp. 36351-36356
    • Tinoco, L.W.1    da Silva, A.2    Leite, A.3    Valente, A.P.4    Almeida, F.C.L.5
  • 30
    • 0033592961 scopus 로고    scopus 로고
    • Structure of the antimicrobial peptide tritripticin bound to micelles: a distinct membrane-bound peptide fold
    • Schibli D.J., Hwang P.M., Vogel H.J. Structure of the antimicrobial peptide tritripticin bound to micelles: a distinct membrane-bound peptide fold. Biochemistry 1999, 38:16749-16755.
    • (1999) Biochemistry , vol.38 , pp. 16749-16755
    • Schibli, D.J.1    Hwang, P.M.2    Vogel, H.J.3
  • 31
    • 65249140613 scopus 로고    scopus 로고
    • Comparison of the membrane interaction mechanism of two antimicrobial RNases: RNase 3/ECP and RNase 7
    • Torrent M., Sánchez D., Buzón V., Nogués M.V., Cladera J., Boix E. Comparison of the membrane interaction mechanism of two antimicrobial RNases: RNase 3/ECP and RNase 7. Biochim. Biophys. Acta 2009, 1788:1116-1125.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1116-1125
    • Torrent, M.1    Sánchez, D.2    Buzón, V.3    Nogués, M.V.4    Cladera, J.5    Boix, E.6
  • 32
    • 16844373772 scopus 로고    scopus 로고
    • Rational design of α-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index
    • Chen Y.C., Mant 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.C.1    Mant, T.2    Farmer, S.W.3    Hancock, R.E.W.4    Vasil, M.L.5    Hodges, R.S.6
  • 34
    • 32944472272 scopus 로고    scopus 로고
    • Interactions between the plasma membrane and the antimicrobial peptide HP (2-20) and its analogues derived from Helicobacter pylori
    • Lee K.H., Lee D.G., Park Y., Kang D., Shin S.Y., Hahm K.S., Kim Y. Interactions between the plasma membrane and the antimicrobial peptide HP (2-20) and its analogues derived from Helicobacter pylori. Biochem. J. 2006, 394:105-114.
    • (2006) Biochem. J. , vol.394 , pp. 105-114
    • Lee, K.H.1    Lee, D.G.2    Park, Y.3    Kang, D.4    Shin, S.Y.5    Hahm, K.S.6    Kim, Y.7
  • 35
    • 23944500330 scopus 로고    scopus 로고
    • Controlled alteratioof the shape and conformational stability of a-helical cell-lytic peptides: effect on mode of action and cell specificity
    • Zelezetsky I., Pacor S., Pag U., Papo N., Shai Y., Sahl H.G., Tossi A. Controlled alteratioof the shape and conformational stability of a-helical cell-lytic peptides: effect on mode of action and cell specificity. Biochem. J. 2005, 390:177-188.
    • (2005) Biochem. J. , vol.390 , pp. 177-188
    • Zelezetsky, I.1    Pacor, S.2    Pag, U.3    Papo, N.4    Shai, Y.5    Sahl, H.G.6    Tossi, A.7
  • 36
    • 0346034649 scopus 로고    scopus 로고
    • Tryptophan rich antimicrobial peptides: comparative properties and membrane interactions
    • Schibli D.J., Epand R.F., Vogel H.J., Epand R.M. Tryptophan rich antimicrobial peptides: comparative properties and membrane interactions. Biochem. Cell Biol. 2002, 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
  • 37
    • 0038385976 scopus 로고    scopus 로고
    • Effect of cholesterol on the properties of phospholipid membranes 1.Structural features
    • Jedlovsky P., Mezei M. Effect of cholesterol on the properties of phospholipid membranes 1.Structural features. J. Phys. Chem. B 2003, 107:5311-5321.
    • (2003) J. Phys. Chem. B , vol.107 , pp. 5311-5321
    • Jedlovsky, P.1    Mezei, M.2
  • 38
    • 0033592458 scopus 로고
    • CD spectra of indolicidin antimicrobial peptides suggest turns, not polyproline helix
    • Ladokhin A.S., Selsted M.E., White S.H. CD spectra of indolicidin antimicrobial peptides suggest turns, not polyproline helix. Biochemistry 1991, 38:12313-12319.
    • (1991) Biochemistry , vol.38 , pp. 12313-12319
    • Ladokhin, A.S.1    Selsted, M.E.2    White, S.H.3
  • 40
    • 0032562219 scopus 로고    scopus 로고
    • Quantitative studies on the melittin-induced leakage mechanism of lipid vesicles
    • Rex S., Schwarz G. Quantitative studies on the melittin-induced leakage mechanism of lipid vesicles. Biochemistry 1998, 37:2336-2345.
    • (1998) Biochemistry , vol.37 , pp. 2336-2345
    • Rex, S.1    Schwarz, G.2
  • 41
    • 69249142709 scopus 로고    scopus 로고
    • Mechanism of antimicrobial, cytolytic, and cell penetrating peptides: from kinetics to thermodynamics
    • Almeida P.F., Pokorny A. Mechanism of antimicrobial, cytolytic, and cell penetrating peptides: from kinetics to thermodynamics. Biochemistry 2009, 48:8083-8093.
    • (2009) Biochemistry , vol.48 , pp. 8083-8093
    • Almeida, P.F.1    Pokorny, A.2
  • 42
    • 38149030149 scopus 로고    scopus 로고
    • Amphipathic alpha-helical peptide, HP (2-20), and its analogues derived from Helicobacter pylori: pore formation mechanism in various lipid compositions
    • Park S.C., Kim M.H., Hossain M.A., Shin S.Y., Kim Y., Stella L., Wade J.D., Park Y., Hahm K.S. Amphipathic alpha-helical peptide, HP (2-20), and its analogues derived from Helicobacter pylori: pore formation mechanism in various lipid compositions. Biochim. Biophys. Acta 2008, 1778:229-241.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 229-241
    • Park, S.C.1    Kim, M.H.2    Hossain, M.A.3    Shin, S.Y.4    Kim, Y.5    Stella, L.6    Wade, J.D.7    Park, Y.8    Hahm, K.S.9
  • 43
    • 52049095275 scopus 로고    scopus 로고
    • s2-casein f(183-207) and effect on bacterial membranes and cell morphology
    • s2-casein f(183-207) and effect on bacterial membranes and cell morphology. Biochim. Biophys. Acta 2008, 1778:2444-2449.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 2444-2449
    • Exposito, I.L.1    Amigo, L.2    Recio, I.3
  • 44
    • 33845958382 scopus 로고    scopus 로고
    • Nisin-induced changes in Bacillus morphology suggests a paradigm of antibiotic action
    • Hyde A.J., Parisot J., McNichol A., Bonev B.B. Nisin-induced changes in Bacillus morphology suggests a paradigm of antibiotic action. Proc. Natl. Acad. Sci. 2006, 103:19896-19901.
    • (2006) Proc. Natl. Acad. Sci. , vol.103 , pp. 19896-19901
    • Hyde, A.J.1    Parisot, J.2    McNichol, A.3    Bonev, B.B.4
  • 47
    • 0032489294 scopus 로고    scopus 로고
    • Mechanism of action of the antimicrobial peptide Buforin II: Buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions
    • Park C.B., Kim H.S., Kim S.C. Mechanism of action of the antimicrobial peptide Buforin II: Buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions. Biochem. Biophys. Res. Commun. 1998, 244:253-257.
    • (1998) Biochem. Biophys. Res. Commun. , vol.244 , pp. 253-257
    • Park, C.B.1    Kim, H.S.2    Kim, S.C.3
  • 48
    • 58749085926 scopus 로고    scopus 로고
    • Magainin 2 in action: distinct modes of membrane permeabilization in living bacterial and mammalian cells
    • Imura Y., Choda N., Matsuzaki K. Magainin 2 in action: distinct modes of membrane permeabilization in living bacterial and mammalian cells. Biophys. J. 2008, 95:5757-5765.
    • (2008) Biophys. J. , vol.95 , pp. 5757-5765
    • Imura, Y.1    Choda, N.2    Matsuzaki, K.3
  • 49
    • 33749071615 scopus 로고    scopus 로고
    • Different modes in antibiotic action of tritripticin analogs, cathelicidin-derived Trp-rich and Pro/Arg-rich peptides
    • Yang S.T., Shin S.Y., Hahm K.S., Kim J.I. Different modes in antibiotic action of tritripticin analogs, cathelicidin-derived Trp-rich and Pro/Arg-rich peptides. Biochim. Biophys. Acta 2006, 1758:1580-1586.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1580-1586
    • Yang, S.T.1    Shin, S.Y.2    Hahm, K.S.3    Kim, J.I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.