메뉴 건너뛰기




Volumn 31, Issue 7, 2010, Pages 1251-1261

Cell selectivity and anti-inflammatory activity of a Leu/Lys-rich α-helical model antimicrobial peptide and its diastereomeric peptides

Author keywords

Anti inflammatory activity; Antimicrobial activity; Cell selectivity; Diastereomeric peptides; Hemolytic activity; Leu Lys rich model antimicrobial peptide

Indexed keywords

ESCHERICHIA COLI LIPOPOLYSACCHARIDE; INDUCIBLE NITRIC OXIDE SYNTHASE; LEUCINE; LYSINE; LYSINE DEXTRO LEUCYLLYSINE DEXTRO LYSYLLEUCINE DEXTRO LEUCYLLYSINE DEXTRO LYSYLTRYPTOPHAN DEXTRO LEUCYLLYSINE DEXTRO LEUCYLLEUCINE DEXTRO LYSYLLYSINE DEXTRO LEUCYLLEUCINE DEXTRO LYSINE AMIDE; LYSYLLEUCINE DEXTRO LYSYLLYSYLLEUCINE DEXTRO LEUCYLLYSYLLYSINE DEXTRO TRYPTOPHANYLLEUCYLLYSINE DEXTRO LEUCYLLEUCYLLYSINE DEXTRO LYSYLLEUCYLLEUCINE DEXTRO LYSINE AMIDE; LYSYLLEUCYLLYSINE DEXTRO LYSYLLEUCYLLEUCYLLYSINE DEXTRO LYSYLTRYPTOPHANYLLEUCYLLYSINE DEXTRO LEUCYLLEUCYLLYSYLLYSINE DEXTRO LEUCYLLEUCYLLYSINE AMIDE; LYSYLLEUCYLLYSYLLYSINE DEXTRO LEUCYLLEUCYLLYSYLLYSYLTRYPTOPHAN DEXTRO LEUCYLLYSYLLEUCYLLEUCYLLYSINE DEXTRO LYSYLLEUCYLLEUCYLLYSINE AMIDE; LYSYLLEUCYLLYSYLLYSYLLEUCINE DEXTRO LEUCYLLYSYLLYSYLTRYPTOPHANYLLEUCYLLYSINE DEXTRO LEUCYLLEUCYLLYSYLLYSYLLEUCYLLEUCINE DEXTRO LYSINE AMIDE; LYSYLLEUCYLLYSYLLYSYLLEUCYLLEUCYLLYSYLLYSYLTRYPTOPHAN DEXTRO LEUCINE DEXTRO LYSINE DEXTRO LEUCINE DEXTRO LEUCINE DEXTRO LYSINE DEXTRO LYSINE DEXTRO LEUCINE DEXTRO LEUCINE DEXTRO LYSINE AMIDE; LYSYLLEUCYLLYSYLLYSYLLEUCYLLEUCYLLYSYLLYSYLTRYPTOPHANYLLEUCYLLYSYLLEUCYLLEUCYLLYSYLLYSYLLEUCYLLEUCYLLYSINE AMIDE; MESSENGER RNA; NITRIC OXIDE; POLYPEPTIDE ANTIBIOTIC AGENT; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

EID: 77952548132     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.peptides.2010.03.032     Document Type: Article
Times cited : (33)

References (38)
  • 1
    • 0034820507 scopus 로고    scopus 로고
    • Bacterial lipopolysaccharides and innate immunity
    • Alexander C., and Rietschel E.T. Bacterial lipopolysaccharides and innate immunity. J Endotoxin Res 7 (2001) 167-202
    • (2001) J Endotoxin Res , vol.7 , pp. 167-202
    • Alexander, C.1    Rietschel, E.T.2
  • 3
    • 16844373772 scopus 로고    scopus 로고
    • Rational design of α-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index
    • Chen Y., Mant C.T., Farmer S.W., Hancock R.E., Vasil M.L., and Hodges R.S. Rational design of α-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index. J Biol Chem 280 (2005) 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
  • 4
    • 0037180768 scopus 로고    scopus 로고
    • The immunopathogenesis of sepsis
    • Cohen J. The immunopathogenesis of sepsis. Nature 420 (2002) 885-891
    • (2002) Nature , vol.420 , pp. 885-891
    • Cohen, J.1
  • 5
    • 0034726410 scopus 로고    scopus 로고
    • Analysis of lipopolysaccharide (LPS)-binding characteristics of serum components using gel filtration of FITC-labeled LPS
    • de Haas C.J., van Leeuwen H.J., Verhoef J., van Kessel K.P., and van Strijp J.A. Analysis of lipopolysaccharide (LPS)-binding characteristics of serum components using gel filtration of FITC-labeled LPS. J Immunol Methods 242 (2000) 79-89
    • (2000) J Immunol Methods , vol.242 , pp. 79-89
    • de Haas, C.J.1    van Leeuwen, H.J.2    Verhoef, J.3    van Kessel, K.P.4    van Strijp, J.A.5
  • 6
    • 34248377855 scopus 로고    scopus 로고
    • Biological and structural characterization of new linear gomesin analogues with improved therapeutic indices
    • Fázio M.A., Jouvensal L., Vovelle F., Bulet P., Miranda M.T., Daffre S., et al. Biological and structural characterization of new linear gomesin analogues with improved therapeutic indices. Biopolymers 88 (2007) 386-400
    • (2007) Biopolymers , vol.88 , pp. 386-400
    • Fázio, M.A.1    Jouvensal, L.2    Vovelle, F.3    Bulet, P.4    Miranda, M.T.5    Daffre, S.6
  • 8
    • 0036445391 scopus 로고    scopus 로고
    • Antimicrobial activity and stability to proteolysis of small linear cationic peptides with d-amino acid substitutions
    • Hamamoto K., Kida Y., Zhang Y., Shimizu T., and Kuwano K. Antimicrobial activity and stability to proteolysis of small linear cationic peptides with d-amino acid substitutions. Microbiol Immunol 46 (2002) 741-749
    • (2002) Microbiol Immunol , vol.46 , pp. 741-749
    • Hamamoto, K.1    Kida, Y.2    Zhang, Y.3    Shimizu, T.4    Kuwano, K.5
  • 9
    • 0035496012 scopus 로고    scopus 로고
    • Cationic peptides: effectors in innate immunity and novel antimicrobials
    • Hancock R.E. Cationic peptides: effectors in innate immunity and novel antimicrobials. Lancet Infect Dis 1 (2001) 156-164
    • (2001) Lancet Infect Dis , vol.1 , pp. 156-164
    • Hancock, R.E.1
  • 10
    • 33845699790 scopus 로고    scopus 로고
    • Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies
    • Hancock R.E., and Sahl H.G. Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat Biotechnol 24 (2006) 1551-1557
    • (2006) Nat Biotechnol , vol.24 , pp. 1551-1557
    • Hancock, R.E.1    Sahl, H.G.2
  • 11
    • 0034255255 scopus 로고    scopus 로고
    • The role of antimicrobial peptides in animal defenses
    • Hancock R.E., and Scott M.G. The role of antimicrobial peptides in animal defenses. Proc Natl Acad Sci USA 97 (2000) 8856-8861
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 8856-8861
    • Hancock, R.E.1    Scott, M.G.2
  • 12
    • 0033592990 scopus 로고    scopus 로고
    • Structure and organization of hemolytic and nonhemolytic diastereomers of antimicrobial peptides in membranes
    • Hong J., Oren Z., and Shai Y. Structure and organization of hemolytic and nonhemolytic diastereomers of antimicrobial peptides in membranes. Biochemistry 38 (1999) 16963-16973
    • (1999) Biochemistry , vol.38 , pp. 16963-16973
    • Hong, J.1    Oren, Z.2    Shai, Y.3
  • 13
    • 0032587536 scopus 로고    scopus 로고
    • Activation of NF-kappaB/Rel in angelan-stimulated macrophages
    • Jeon Y.J., Han S.B., Ahn K.S., and Kim H.M. Activation of NF-kappaB/Rel in angelan-stimulated macrophages. Immunopharmacology 43 (1999) 1-9
    • (1999) Immunopharmacology , vol.43 , pp. 1-9
    • Jeon, Y.J.1    Han, S.B.2    Ahn, K.S.3    Kim, H.M.4
  • 14
    • 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 S.S., and Lee B.J. Correlation between the activities of α-helical antimicrobial peptides and hydrophobicities represented as RP-HPLC retention times. Peptides 26 (2005) 2050-2056
    • (2005) Peptides , vol.26 , pp. 2050-2056
    • Kim, S.1    Kim, S.S.2    Lee, B.J.3
  • 15
    • 0029797094 scopus 로고    scopus 로고
    • Design and synthesis of amphiphilic α-helical model peptides with systematically varied hydrophobic-hydrophilic balance and their interaction with lipid- and bio-membranes
    • Kiyota T., Lee S., and Sugihara G. Design and synthesis of amphiphilic α-helical model peptides with systematically varied hydrophobic-hydrophilic balance and their interaction with lipid- and bio-membranes. Biochemistry 35 (1996) 13196-13204
    • (1996) Biochemistry , vol.35 , pp. 13196-13204
    • Kiyota, T.1    Lee, S.2    Sugihara, G.3
  • 16
    • 0033613815 scopus 로고    scopus 로고
    • Folding of amphipathic α-helices on membranes: energetics of helix formation by melittin
    • Ladokhin A.S., and White S.H. Folding of amphipathic α-helices on membranes: energetics of helix formation by melittin. J Mol Biol 285 (1999) 1363-1369
    • (1999) J Mol Biol , vol.285 , pp. 1363-1369
    • Ladokhin, A.S.1    White, S.H.2
  • 17
    • 1542511360 scopus 로고    scopus 로고
    • Effects of single d-amino acid substitutions on disruption of β-sheet structure and hydrophobicity in cyclic 14-residue antimicrobial peptide analogs related to gramicidin S
    • Lee D.L., Powers J.P., Pflegerl K., Vasil M.L., Hancock R.E.W., and Hodges R.S. Effects of single d-amino acid substitutions on disruption of β-sheet structure and hydrophobicity in cyclic 14-residue antimicrobial peptide analogs related to gramicidin S. J Pept Res 63 (2004) 69-84
    • (2004) J Pept Res , vol.63 , pp. 69-84
    • Lee, D.L.1    Powers, J.P.2    Pflegerl, K.3    Vasil, M.L.4    Hancock, R.E.W.5    Hodges, R.S.6
  • 18
    • 0021755639 scopus 로고
    • Differential light scattering and absorption flattening optical effects are minimal in the circular dichroism spectra of small unilamellar vesicles
    • Mao D., and Wallace B.A. Differential light scattering and absorption flattening optical effects are minimal in the circular dichroism spectra of small unilamellar vesicles. Biochemistry 23 (1984) 2667-2673
    • (1984) Biochemistry , vol.23 , pp. 2667-2673
    • Mao, D.1    Wallace, B.A.2
  • 19
    • 0031005930 scopus 로고    scopus 로고
    • A repertoire of novel antibacterial diastereomeric peptides with selective cytolytic activity
    • Oren Z., Hong J., and Shai Y. A repertoire of novel antibacterial diastereomeric peptides with selective cytolytic activity. J Biol Chem 272 (1997) 14643-14649
    • (1997) J Biol Chem , vol.272 , pp. 14643-14649
    • Oren, Z.1    Hong, J.2    Shai, Y.3
  • 20
    • 0031024551 scopus 로고    scopus 로고
    • Selective lysis of bacteria but not mammalian cells by diastereomers of melittin: structure-function study
    • Oren Z., and Shai Y. Selective lysis of bacteria but not mammalian cells by diastereomers of melittin: structure-function study. Biochemistry 36 (1997) 1826-1835
    • (1997) Biochemistry , vol.36 , pp. 1826-1835
    • Oren, Z.1    Shai, Y.2
  • 21
    • 0037072808 scopus 로고    scopus 로고
    • The consequence of sequence alteration of an amphipathic α-helical antimicrobial peptide and its diastereomers
    • Papo N., Oren Z., Pag U., Sahl H.G., and Shai Y. The consequence of sequence alteration of an amphipathic α-helical antimicrobial peptide and its diastereomers. J Biol Chem 277 (2002) 33913-33921
    • (2002) J Biol Chem , vol.277 , pp. 33913-33921
    • Papo, N.1    Oren, Z.2    Pag, U.3    Sahl, H.G.4    Shai, Y.5
  • 22
    • 33644978944 scopus 로고    scopus 로고
    • Endotoxin (lipopolysaccharide) neutralization by innate immunity host-defense peptides. Peptide properties and plausible modes of action
    • Rosenfeld Y., Papo N., and Shai Y. Endotoxin (lipopolysaccharide) neutralization by innate immunity host-defense peptides. Peptide properties and plausible modes of action. J Biol Chem 281 (2006) 1636-1643
    • (2006) J Biol Chem , vol.281 , pp. 1636-1643
    • Rosenfeld, Y.1    Papo, N.2    Shai, Y.3
  • 23
    • 0344198180 scopus 로고    scopus 로고
    • Structure-based design of an indolicidin peptide analogue with increased protease stability
    • Rozek A., Powers J.P., Friedrich C.L., and Hancock R.E. Structure-based design of an indolicidin peptide analogue with increased protease stability. Biochemistry 42 (2003) 14130-14138
    • (2003) Biochemistry , vol.42 , pp. 14130-14138
    • Rozek, A.1    Powers, J.P.2    Friedrich, C.L.3    Hancock, R.E.4
  • 24
    • 0023792919 scopus 로고
    • Evaluation of a soluble tetrazolium/formazan assay for cell growth and drug sensitivity in culture using human and other tumor cell lines
    • Scudiero D.A., Shoemaker R.H., Paull K.D., Monks A., Tierney S., Nofziger T.H., et al. Evaluation of a soluble tetrazolium/formazan assay for cell growth and drug sensitivity in culture using human and other tumor cell lines. Cancer Res 48 (1988) 4827-4833
    • (1988) Cancer Res , vol.48 , pp. 4827-4833
    • Scudiero, D.A.1    Shoemaker, R.H.2    Paull, K.D.3    Monks, A.4    Tierney, S.5    Nofziger, T.H.6
  • 25
    • 0025245504 scopus 로고
    • Channel formation properties of synthetic pardaxin and analogues
    • Shai Y., Bach D., and Yanovsky A. Channel formation properties of synthetic pardaxin and analogues. J Biol Chem 265 (1990) 20202-20209
    • (1990) J Biol Chem , vol.265 , pp. 20202-20209
    • Shai, Y.1    Bach, D.2    Yanovsky, A.3
  • 26
    • 0029665072 scopus 로고    scopus 로고
    • Diastereoisomers of cytolysins, a novel class of potent antibacterial peptides
    • Shai Y., and Oren Z. Diastereoisomers of cytolysins, a novel class of potent antibacterial peptides. J Biol Chem 271 (1996) 7305-7308
    • (1996) J Biol Chem , vol.271 , pp. 7305-7308
    • Shai, Y.1    Oren, Z.2
  • 27
    • 0033576264 scopus 로고    scopus 로고
    • 2D-NMR and ATR-FTIR study of the structure of a cell-selective diastereomer of melittin and its orientation in phospholipids
    • Sharon M., Oren Z., Shai Y., and Anglister J. 2D-NMR and ATR-FTIR study of the structure of a cell-selective diastereomer of melittin and its orientation in phospholipids. Biochemistry 38 (1999) 15305-15316
    • (1999) Biochemistry , vol.38 , pp. 15305-15316
    • Sharon, M.1    Oren, Z.2    Shai, Y.3    Anglister, J.4
  • 28
    • 0016377375 scopus 로고
    • Lipid composition as a guide to the classification of bacteria
    • Shaw N. Lipid composition as a guide to the classification of bacteria. Adv Appl Microbiol 117 (1974) 63-108
    • (1974) Adv Appl Microbiol , vol.117 , pp. 63-108
    • Shaw, N.1
  • 30
    • 24644516579 scopus 로고    scopus 로고
    • Cell selectivity and mechanism of action of antimicrobial model peptides containing peptoid residues
    • Song Y.M., Park Y., Lim S.S., Yang S.T., Woo E.R., Park I.S., et al. Cell selectivity and mechanism of action of antimicrobial model peptides containing peptoid residues. Biochemistry 44 (2005) 12094-12106
    • (2005) Biochemistry , vol.44 , pp. 12094-12106
    • Song, Y.M.1    Park, Y.2    Lim, S.S.3    Yang, S.T.4    Woo, E.R.5    Park, I.S.6
  • 31
    • 0028157442 scopus 로고
    • Monomeric Re lipopolysaccharide from Escherichia coli is more active than the aggregated form in the Limulus amebocyte lysate assay and in inducing Egr-1 mRNA in murine peritoneal macrophages
    • Takayama K., Mitchell D.H., Din Z.Z., Mukerjee P., Li C., and Coleman D.L. Monomeric Re lipopolysaccharide from Escherichia coli is more active than the aggregated form in the Limulus amebocyte lysate assay and in inducing Egr-1 mRNA in murine peritoneal macrophages. J Biol Chem 269 (1994) 2241-2244
    • (1994) J Biol Chem , vol.269 , pp. 2241-2244
    • Takayama, K.1    Mitchell, D.H.2    Din, Z.Z.3    Mukerjee, P.4    Li, C.5    Coleman, D.L.6
  • 32
    • 0028924539 scopus 로고
    • Lipopolysaccharide binding protein-mediated complexation of lipopolysaccharide with soluble CD14
    • Tobias P.S., Soldau K., Gegner J.A., Mintz D., and Ulevitch R.J. Lipopolysaccharide binding protein-mediated complexation of lipopolysaccharide with soluble CD14. J Biol Chem 270 (1995) 10482-10488
    • (1995) J Biol Chem , vol.270 , pp. 10482-10488
    • Tobias, P.S.1    Soldau, K.2    Gegner, J.A.3    Mintz, D.4    Ulevitch, R.J.5
  • 33
    • 0027318570 scopus 로고
    • Lipopolysaccharide binding protein and CD14 in LPS dependent macrophage activation
    • Tobias P.S., and Ulevitch R.J. Lipopolysaccharide binding protein and CD14 in LPS dependent macrophage activation. Immunobiology 187 (1993) 227-232
    • (1993) Immunobiology , vol.187 , pp. 227-232
    • Tobias, P.S.1    Ulevitch, R.J.2
  • 34
    • 0015821003 scopus 로고
    • The asymmetric distribution of phospholipids in the human red cell membrane. A combined study using phospholipases and freeze-etch electron microscopy
    • Verkleij A.J., Zwaal R.F., Roelofsen B., Comfurius P., Kastelijn D., and Deenen L.V. The asymmetric distribution of phospholipids in the human red cell membrane. A combined study using phospholipases and freeze-etch electron microscopy. Biochim Biophys Acta 323 (1973) 178-193
    • (1973) Biochim Biophys Acta , vol.323 , pp. 178-193
    • Verkleij, A.J.1    Zwaal, R.F.2    Roelofsen, B.3    Comfurius, P.4    Kastelijn, D.5    Deenen, L.V.6
  • 35
    • 0030957876 scopus 로고    scopus 로고
    • Peptide hydrophobicity controls the activity and selectivity of magainin 2 amide in interaction with membranes
    • Wieprecht T., Dathe M., Beyermann M., Krause E., Maloy W.L., MacDonald D.L., et al. Peptide hydrophobicity controls the activity and selectivity of magainin 2 amide in interaction with membranes. Biochemistry 36 (1997) 6124-6132
    • (1997) Biochemistry , vol.36 , pp. 6124-6132
    • Wieprecht, T.1    Dathe, M.2    Beyermann, M.3    Krause, E.4    Maloy, W.L.5    MacDonald, D.L.6
  • 36
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 415 (2002) 389-395
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 37
    • 36949003906 scopus 로고    scopus 로고
    • Cell selectivity of an antimicrobial peptide melittin diastereomer with d-amino acid in the leucine zipper sequence
    • Zhu W.L., Nan Y.H., Hahm K.S., and Shin S.Y. Cell selectivity of an antimicrobial peptide melittin diastereomer with d-amino acid in the leucine zipper sequence. J Biochem Mol Biol 40 (2007) 1090-1094
    • (2007) J Biochem Mol Biol , vol.40 , pp. 1090-1094
    • Zhu, W.L.1    Nan, Y.H.2    Hahm, K.S.3    Shin, S.Y.4
  • 38
    • 23844523180 scopus 로고    scopus 로고
    • Antimicrobial peptides and endotoxin inhibit cytokine and nitric oxide release but amplify respiratory burst response in human and murine macrophages
    • Zughaier S.M., Shafer W.M., and Stephens D.S. Antimicrobial peptides and endotoxin inhibit cytokine and nitric oxide release but amplify respiratory burst response in human and murine macrophages. Cell Microbiol 7 (2005) 1251-1262
    • (2005) Cell Microbiol , vol.7 , pp. 1251-1262
    • Zughaier, S.M.1    Shafer, W.M.2    Stephens, D.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.