메뉴 건너뛰기




Volumn 28, Issue 8-9, 2011, Pages 537-555

Glycosylated analogs of formaecin I and drosocin exhibit differential pattern of antibacterial activity

Author keywords

Antibacterial activity; Drosocin; Formaecin I; Glycosylated peptides; Synthesis

Indexed keywords

ANTIINFECTIVE AGENT; DROSOCIN; FORMAECIN 1 PROTEIN, MYRMECIA GULOSA; GLYCOPEPTIDE; GLYCOPROTEIN; INSECT PROTEIN;

EID: 84863800481     PISSN: 02820080     EISSN: 15734986     Source Type: Journal    
DOI: 10.1007/s10719-011-9353-2     Document Type: Article
Times cited : (34)

References (50)
  • 1
    • 0034505430 scopus 로고    scopus 로고
    • Synthesis of complex carbohydrates and glycoconjugates: Enzyme-based and programmable one-pot strategies
    • Koeller, K.M., Wong, C.H.: Synthesis of complex carbohydrates and glycoconjugates: Enzyme-based and programmable one-pot strategies. Chem. Rev. 100(12), 4465-4494 (2000)
    • (2000) Chem. Rev. , vol.100 , Issue.12 , pp. 4465-4494
    • Koeller, K.M.1    Wong, C.H.2
  • 2
    • 33749071408 scopus 로고    scopus 로고
    • Structural aspects of glycomes with a focus on N-glycosylation and glycoprotein folding
    • Petrescu, A.J., Wormald, M.R., Dwek, R.A.: Structural aspects of glycomes with a focus on N-glycosylation and glycoprotein folding. Curr. Opin. Struct. Biol. 16(5), 600-607 (2006)
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , Issue.5 , pp. 600-607
    • Petrescu, A.J.1    Wormald, M.R.2    Dwek, R.A.3
  • 3
    • 53849101862 scopus 로고    scopus 로고
    • Expeditious chemoenzymatic synthesis of homogeneous N-glycoproteins carrying defined oligosaccharide ligands
    • Ochiai, H., Huang, W., Wang, L.X.: Expeditious chemoenzymatic synthesis of homogeneous N-glycoproteins carrying defined oligosaccharide ligands. J. Am. Chem. Soc. 130(41), 13790-13803 (2008)
    • (2008) J. Am. Chem. Soc. , vol.130 , Issue.41 , pp. 13790-13803
    • Ochiai, H.1    Huang, W.2    Wang, L.X.3
  • 4
    • 0032727842 scopus 로고    scopus 로고
    • Effect of N-linked glycosylation on glycopeptide and glycoprotein structure
    • Imperiali, B., O'Connor, S.E.: Effect of N-linked glycosylation on glycopeptide and glycoprotein structure. Curr. Opin. Chem. Biol. 3(6), 643-649 (1999)
    • (1999) Curr. Opin. Chem. Biol. , vol.3 , Issue.6 , pp. 643-649
    • Imperiali, B.1    O'Connor, S.E.2
  • 5
    • 35248882544 scopus 로고    scopus 로고
    • Modulation of protein biophysical properties by chemical glycosylation: Biochemical insights and biomedical implications
    • Sola, R.J., Rodriguez-Martinez, J.A., Griebenow, K.: Modulation of protein biophysical properties by chemical glycosylation: Biochemical insights and biomedical implications. Cell. Mol. Life Sci. 64(16), 2133-2152 (2007)
    • (2007) Cell. Mol. Life Sci. , vol.64 , Issue.16 , pp. 2133-2152
    • Sola, R.J.1    Rodriguez-Martinez, J.A.2    Griebenow, K.3
  • 6
    • 0035937505 scopus 로고    scopus 로고
    • Intracellular functions of N-linked glycans
    • Helenius, A., Aebi, M.: Intracellular functions of N-linked glycans. Science 291(5512), 2364-2369 (2001)
    • (2001) Science , vol.291 , Issue.5512 , pp. 2364-2369
    • Helenius, A.1    Aebi, M.2
  • 7
    • 0033614823 scopus 로고    scopus 로고
    • Effects of glycosylation on the structure and dynamics of eel calcitonin in micelles and lipid bilayers determined by nuclear magnetic resonance spectroscopy
    • Hashimoto, Y., Toma, K., Nishikido, J., Yamamoto, K., Haneda, K., Inazu, T., Valentine, K.G., Opella, S.J.: Effects of glycosylation on the structure and dynamics of eel calcitonin in micelles and lipid bilayers determined by nuclear magnetic resonance spectroscopy. Biochemistry 38(26), 8377-8384 (1999)
    • (1999) Biochemistry , vol.38 , Issue.26 , pp. 8377-8384
    • Hashimoto, Y.1    Toma, K.2    Nishikido, J.3    Yamamoto, K.4    Haneda, K.5    Inazu, T.6    Valentine, K.G.7    Opella, S.J.8
  • 8
    • 0000300894 scopus 로고
    • Structure and dynamics of a synthetic O-glycosylated cyclopeptide in solution determined by NMR spectroscopy and MD simulations
    • Kessler, H., Matter, H., Gemmecker, G., Kottenhahn, M., Bates, J. W.: Structure and dynamics of a synthetic O-glycosylated cyclopeptide in solution determined by NMR spectroscopy and MD simulations. J. Am. Chem. Soc. 114, 4805-4818 (1992)
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 4805-4818
    • Kessler, H.1    Matter, H.2    Gemmecker, G.3    Kottenhahn, M.4    Bates, J.W.5
  • 9
    • 0024389522 scopus 로고
    • Role of glycosylation on the conformation and chain dimensions of O-linked glycoproteins: Light-scattering studies of ovine submaxillary mucin
    • Shogren, R., Gerken, T.A., Jentoft, N.: Role of glycosylation on the conformation and chain dimensions of O-linked glycoproteins: Light-scattering studies of ovine submaxillary mucin. Biochemistry 28(13), 5525-5536 (1989)
    • (1989) Biochemistry , vol.28 , Issue.13 , pp. 5525-5536
    • Shogren, R.1    Gerken, T.A.2    Jentoft, N.3
  • 10
    • 0024319438 scopus 로고
    • Effects of glycosylation on the conformation and dynamics of O-linked glycoproteins: Carbon-13 NMR studies of ovine submaxillary mucin
    • Gerken, T.A., Butenhof, K.J., Shogren, R.: Effects of glycosylation on the conformation and dynamics of O-linked glycoproteins: Carbon-13 NMR studies of ovine submaxillary mucin. Biochemistry 28(13), 5536-5543 (1989)
    • (1989) Biochemistry , vol.28 , Issue.13 , pp. 5536-5543
    • Gerken, T.A.1    Butenhof, K.J.2    Shogren, R.3
  • 11
    • 0026337737 scopus 로고
    • Structure of a legume lectin with an ordered N-linked carbohydrate in complex with lactose
    • Shaanan, B., Lis, H., Sharon, N.: Structure of a legume lectin with an ordered N-linked carbohydrate in complex with lactose. Science 254(5033), 862-866 (1991)
    • (1991) Science , vol.254 , Issue.5033 , pp. 862-866
    • Shaanan, B.1    Lis, H.2    Sharon, N.3
  • 12
    • 0026624745 scopus 로고
    • Effects of glycosylation on protein conformation and amide proton exchange rates in RNase B
    • Joao, H.C., Scragg, I.G., Dwek, R.A.: Effects of glycosylation on protein conformation and amide proton exchange rates in RNase B. FEBS Lett. 307(3), 343-346 (1992)
    • (1992) FEBS Lett. , vol.307 , Issue.3 , pp. 343-346
    • Joao, H.C.1    Scragg, I.G.2    Dwek, R.A.3
  • 13
    • 13344291142 scopus 로고
    • Effect of glycosylation on peptide backbone conformation
    • Andreotti, A.H., Kahne, D.: Effect of glycosylation on peptide backbone conformation. J. Am. Chem. Soc. 115, 3352-3353 (1993)
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 3352-3353
    • Andreotti, A.H.1    Kahne, D.2
  • 15
    • 0032513209 scopus 로고    scopus 로고
    • Isolation from an ant Myrmecia gulosa of two inducible Oglycosylated proline-rich antibacterial peptides
    • Mackintosh, J.A., Veal, D.A., Beattie, A.J., Gooley, A.A.: Isolation from an ant Myrmecia gulosa of two inducible Oglycosylated proline-rich antibacterial peptides. J. Biol. Chem. 273(11), 6139-6143 (1998)
    • (1998) J. Biol. Chem. , vol.273 , Issue.11 , pp. 6139-6143
    • Mackintosh, J.A.1    Veal, D.A.2    Beattie, A.J.3    Gooley, A.A.4
  • 17
    • 0029051008 scopus 로고
    • A novel antibacterial peptide family isolated from the silkworm bombyx mori
    • Hara, S., Yamakawa, M.: A novel antibacterial peptide family isolated from the silkworm, Bombyx mori. Biochem. J. 310(Pt 2), 651-656 (1995)
    • (1995) Biochem. J. , vol.310 , Issue.PART 2 , pp. 651-656
    • Hara, S.1    Yamakawa, M.2
  • 18
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff, M.: Antimicrobial peptides of multicellular organisms. Nature 415(6870), 389-395 (2002)
    • (2002) Nature , vol.415 , Issue.6870 , pp. 389-395
    • Zasloff, M.1
  • 19
    • 1642545489 scopus 로고    scopus 로고
    • Anti-microbial peptides: From invertebrates to vertebrates
    • Bulet, P., Stocklin, R., Menin, L.: Anti-microbial peptides: From invertebrates to vertebrates. Immunol. Rev. 198, 169-184 (2004)
    • (2004) Immunol. Rev. , vol.198 , pp. 169-184
    • Bulet, P.1    Stocklin, R.2    Menin, L.3
  • 21
    • 0032748297 scopus 로고    scopus 로고
    • Lethal effects of apidaecin on Escherichia coli involve sequentialmolecular interactions with diverse targets
    • Castle, M., Nazarian, A., Yi, S.S., Tempst, P.: Lethal effects of apidaecin on Escherichia coli involve sequentialmolecular interactions with diverse targets. J. Biol. Chem. 274(46), 32555-32564 (1999)
    • (1999) J. Biol. Chem. , vol.274 , Issue.46 , pp. 32555-32564
    • Castle, M.1    Nazarian, A.2    Yi, S.S.3    Tempst, P.4
  • 23
    • 0036633301 scopus 로고    scopus 로고
    • The short proline-rich antibacterial peptide family
    • Otvos Jr., L.: The short proline-rich antibacterial peptide family. Cell. Mol. Life Sci. 59(7), 1138-1150 (2002)
    • (2002) Cell. Mol. Life Sci. , vol.59 , Issue.7 , pp. 1138-1150
    • Otvos Jr., L.1
  • 24
    • 0033547753 scopus 로고    scopus 로고
    • Conformational studies by NMR of the antimicrobial peptide, drosocin, and its non-glycosylated derivative: Effects of glycosylation on solution conformation
    • McManus, A.M., Otvos Jr., L., Hoffmann, R., Craik, D.J.: Conformational studies by NMR of the antimicrobial peptide, drosocin, and its non-glycosylated derivative: Effects of glycosylation on solution conformation. Biochemistry 38(2), 705-714 (1999)
    • (1999) Biochemistry , vol.38 , Issue.2 , pp. 705-714
    • McManus, A.M.1    Otvos Jr., L.2    Hoffmann, R.3    Craik, D.J.4
  • 25
    • 33846482527 scopus 로고    scopus 로고
    • Design of a functionally equivalent nonglycosylated analog of the glycopeptide antibiotic formaecin I
    • Kaur, K.J., Pandey, S., Salunke, D.M.: Design of a functionally equivalent nonglycosylated analog of the glycopeptide antibiotic formaecin I. Protein Sci. 16(2), 309-315 (2007)
    • (2007) Protein Sci. , vol.16 , Issue.2 , pp. 309-315
    • Kaur, K.J.1    Pandey, S.2    Salunke, D.M.3
  • 26
    • 0029929079 scopus 로고    scopus 로고
    • Enlarged scale chemical synthesis and range of activity of drosocin, an Oglycosylated antibacterial peptide of drosophila
    • Bulet, P., Urge, L., Ohresser, S., Hetru, C., Otvos Jr., L.: Enlarged scale chemical synthesis and range of activity of drosocin, an Oglycosylated antibacterial peptide of drosophila. Eur. J. Biochem. 238(1), 64-69 (1996)
    • (1996) Eur. J. Biochem. , vol.238 , Issue.1 , pp. 64-69
    • Bulet, P.1    Urge, L.2    Ohresser, S.3    Hetru, C.4    Otvos Jr., L.5
  • 27
    • 0032992923 scopus 로고    scopus 로고
    • Range of activity and metabolic stability of synthetic antibacterial glycopeptides from insects
    • Hoffmann, R., Bulet, P., Urge, L., Otvos Jr., L.: Range of activity and metabolic stability of synthetic antibacterial glycopeptides from insects. Biochim. Biophys. Acta 1426(3), 459-467 (1999)
    • (1999) Biochim. Biophys. Acta , vol.1426 , Issue.3 , pp. 459-467
    • Hoffmann, R.1    Bulet, P.2    Urge, L.3    Otvos Jr., L.4
  • 28
    • 0000205069 scopus 로고
    • The azidonitration of tri-O-acetyl-D-galactal
    • Synthesis of 2-amino-2-deoxyglycoses and 2-amino-2-deoxyglycosides from glycals. March 1980, U.S. Patent no 4195 174
    • Lemieux, R.U., Ratcliffe, R.M.: The azidonitration of tri-O-acetyl-D-galactal. Can J Chem 57, 1244-1251 (1979). Synthesis of 2-amino-2-deoxyglycoses and 2-amino-2-deoxyglycosides from glycals. March 1980, U.S. Patent no. 4,195,174
    • (1979) Can J Chem , vol.57 , pp. 1244-1251
    • Lemieux, R.U.1    Ratcliffe, R.M.2
  • 29
    • 33846519966 scopus 로고    scopus 로고
    • Recent trends in the synthesis of O-glycosides of 2-amino-2-deoxysugars
    • Bongat, A.F.G., Demchenko, A.V.: Recent trends in the synthesis of O-glycosides of 2-amino-2-deoxysugars. Carbohydr. Res. 342, 374-406 (2007)
    • (2007) Carbohydr. Res. , vol.342 , pp. 374-406
    • Bongat, A.F.G.1    Demchenko, A.V.2
  • 30
    • 0018812791 scopus 로고
    • Preparation and properties of Na-9-fluorenylmethyloxycarbonylamino acids bearing tert-butyl side chain protection
    • Chang, C.D., Waki, M., Ahmad, M., Meienhofer, J., Lundell, E.O., Huag, J.D.: Preparation and properties of Na-9-fluorenylmethyloxycarbonylamino acids bearing tert-butyl side chain protection. Int. J. Pept. Protein Res. 15, 59-66 (1980)
    • (1980) Int. J. Pept. Protein Res. , vol.15 , pp. 59-66
    • Chang, C.D.1    Waki, M.2    Ahmad, M.3    Meienhofer, J.4    Lundell, E.O.5    Huag, J.D.6
  • 31
    • 0033533481 scopus 로고    scopus 로고
    • A chemically synthesized version of the insect antibacterial glycopeptide, diptericin, disrupts bacterial membrane integrity
    • Winans, K.A., King, D.S., Rao, V.R., Bertozzi, C.R.: A chemically synthesized version of the insect antibacterial glycopeptide, diptericin, disrupts bacterial membrane integrity. Biochemistry 38(36), 11700-11710 (1999)
    • (1999) Biochemistry , vol.38 , Issue.36 , pp. 11700-11710
    • Winans, K.A.1    King, D.S.2    Rao, V.R.3    Bertozzi, C.R.4
  • 32
    • 0032501470 scopus 로고    scopus 로고
    • Synthetic and immunological studies on clustered modes of mucin-related Tn and TF Olinked antigens: The preparation of a glycopeptide-basedvaccine for clinical trials against prostate cancer
    • Kuduk, S.D., Schwarz, J.B., Chen, X.T., Glunz, P.W., Raghupathi, G., Livingston, P.O., Danishefsky, S.J.: Synthetic and immunological studies on clustered modes of mucin-related Tn and TF Olinked antigens: The preparation of a glycopeptide-basedvaccine for clinical trials against prostate cancer. J. Am. Chem. Soc. 120 (48), 12474-12485 (1998)
    • (1998) J. Am. Chem. Soc. , vol.120 , Issue.48 , pp. 12474-12485
    • Kuduk, S.D.1    Schwarz, J.B.2    Chen, X.T.3    Glunz, P.W.4    Raghupathi, G.5    Livingston, P.O.6    Danishefsky, S.J.7
  • 34
    • 0033595880 scopus 로고    scopus 로고
    • Synthesis of targetable cationic amphiphiles
    • Ren, T., Liu, D.: Synthesis of targetable cationic amphiphiles. Tetrahedron Lett. 40, 7621-7625 (1999)
    • (1999) Tetrahedron Lett. , vol.40 , pp. 7621-7625
    • Ren, T.1    Liu, D.2
  • 35
    • 84981757672 scopus 로고
    • Some derivatives of grape sugars and galactose
    • Koenigs, W., Knorr, E.: Some derivatives of grape sugars and galactose. Ber 34, 957-981 (1901)
    • (1901) Ber , vol.34 , pp. 957-981
    • Koenigs, W.1    Knorr, E.2
  • 36
    • 0035815155 scopus 로고    scopus 로고
    • Solid-phase synthesis of O-linked glycopeptide analogues of enkephalin
    • Mitchell, S.A., Pratt, M.R., Hruby, V.J., Polt, R.: Solid-phase synthesis of O-linked glycopeptide analogues of enkephalin. J. Org. Chem. 66(7), 2327-2342 (2001)
    • (2001) J. Org. Chem. , vol.66 , Issue.7 , pp. 2327-2342
    • Mitchell, S.A.1    Pratt, M.R.2    Hruby, V.J.3    Polt, R.4
  • 38
    • 0027419529 scopus 로고
    • The evaluation of type I and type II beta-turn mixtures. Circular dichroism, NMR and molecular dynamics studies
    • Perczel, A., Hollosi, M., Sandor, P., Fasman, G.D.: The evaluation of type I and type II beta-turn mixtures. Circular dichroism, NMR and molecular dynamics studies. Int. J. Pept. Protein Res. 41(3), 223-236 (1993)
    • (1993) Int. J. Pept. Protein Res. , vol.41 , Issue.3 , pp. 223-236
    • Perczel, A.1    Hollosi, M.2    Sandor, P.3    Fasman, G.D.4
  • 39
    • 0002940495 scopus 로고
    • Blout, E.R., Bovery, F.A., Goodman, M., Lotan, M. (eds.), Wiley, New York
    • Woody, R.W.: In: Blout, E.R., Bovery, F.A., Goodman, M., Lotan, M. (eds.) Peptides, polypeptides and proteins, pp. 338-360. Wiley, New York (1974)
    • (1974) Peptides, Polypeptides and Proteins , pp. 338-360
    • Woody, R.W.1
  • 40
    • 0001346959 scopus 로고
    • Sensitivity of glycopeptides conformation to carbohydrate chain length
    • Liang, R., Andreotti, A.H., Kahne, D.: Sensitivity of glycopeptides conformation to carbohydrate chain length. J. Am. Chem. Soc. 117, 10395-10396 (1995)
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 10395-10396
    • Liang, R.1    Andreotti, A.H.2    Kahne, D.3
  • 41
    • 0030065240 scopus 로고    scopus 로고
    • Stabilization of proteins by glycosylation examined by NMR analysis of a fucosylated proteinase inhibitor
    • Mer, G., Hietter, H., Lefevre, J.F.: Stabilization of proteins by glycosylation examined by NMR analysis of a fucosylated proteinase inhibitor. Nat. Struct. Biol. 3(1), 45-53 (1996)
    • (1996) Nat. Struct. Biol. , vol.3 , Issue.1 , pp. 45-53
    • Mer, G.1    Hietter, H.2    Lefevre, J.F.3
  • 43
    • 0032807375 scopus 로고    scopus 로고
    • NMR and molecular modeling studies on two glycopeptides fromthe carbohydrate-protein linkage region of connective tissue proteoglycans
    • Agrawal, P.K., Jacquinet, J.C., Krishna, N.R.: NMR and molecular modeling studies on two glycopeptides fromthe carbohydrate-protein linkage region of connective tissue proteoglycans. Glycobiology 9, 669-677 (1999)
    • (1999) Glycobiology , vol.9 , pp. 669-677
    • Agrawal, P.K.1    Jacquinet, J.C.2    Krishna, N.R.3
  • 44
    • 0033599579 scopus 로고    scopus 로고
    • Structural study on O-glycopeptides: Glycosylation-induced conformational changes of O-GlcNAc, OLacNAc, O-Sialyl-LacNAc, and O-Sialyl-Lewis-X peptides of the mucin domain of MAdCAM-1
    • Wu, W.G., Pasternack, L., Huang, D.H., Koeller, M.K., Lin, C.C., Seitz, O., Wong, C.H.: Structural study on O-glycopeptides: Glycosylation-induced conformational changes of O-GlcNAc, OLacNAc, O-Sialyl-LacNAc, and O-Sialyl-Lewis-X peptides of the mucin domain of MAdCAM-1. J. Am. Chem. Soc. 121, 2409-2417 (1999)
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 2409-2417
    • Wu, W.G.1    Pasternack, L.2    Huang, D.H.3    Koeller, M.K.4    Lin, C.C.5    Seitz, O.6    Wong, C.H.7
  • 45
    • 0030745180 scopus 로고    scopus 로고
    • NMR investigations of the role of the sugar moiety in glycosylated recombinant human granulocytecolony-stimulating factor
    • Gervais, V., Zerial, A., Oschkinat, H.:NMR investigations of the role of the sugar moiety in glycosylated recombinant human granulocytecolony-stimulating factor. Eur. J. Biochem. 247(1), 386-395 (1997)
    • (1997) Eur. J. Biochem. , vol.247 , Issue.1 , pp. 386-395
    • Gervais, V.1    Zerial, A.2    Oschkinat, H.3
  • 47
    • 0032544933 scopus 로고    scopus 로고
    • Glycosylation of threonine of the repeating unit of RNA polymerase II with alinked N-acetylglucosamine leads to a turnlike structure
    • Simanek, E.F., Huang, D.H., Pasternack, L., Machajewsky, T.D., Seitz, O., Millar, D.S., Dyson, H.J., Wong, C.H.: Glycosylation of threonine of the repeating unit of RNA polymerase II with alinked N-acetylglucosamine leads to a turnlike structure. J. Am. Chem. Soc. 120, 11567-11575 (1998)
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 11567-11575
    • Simanek, E.F.1    Huang, D.H.2    Pasternack, L.3    Machajewsky, T.D.4    Seitz, O.5    Millar, D.S.6    Dyson, H.J.7    Wong, C.H.8
  • 48
    • 0037403301 scopus 로고    scopus 로고
    • Practical synthesis of the 2-acetamido-3 ,4,6-tri-O-acetyl-2-deoxy-b- Dglucosides of Fmoc-serine and Fmoc-threonine and their benzyl esters
    • Carvalho, I., Scheuerl, S.L., Kartha, K.P.R., Field, R.A.: Practical synthesis of the 2-acetamido-3,4,6-tri-O-acetyl-2-deoxy-b-Dglucosides of Fmoc-serine and Fmoc-threonine and their benzyl esters. Carbohydr. Res. 338, 1039-1043 (2003)
    • (2003) Carbohydr. Res. , vol.338 , pp. 1039-1043
    • Carvalho, I.1    Scheuerl, S.L.2    Kartha, K.P.R.3    Field, R.A.4
  • 49
    • 0033551685 scopus 로고    scopus 로고
    • Structurefunction analysis of tritrypticin, an antibacterial peptide of innate immune origin
    • Nagpal, S., Gupta, V., Kaur, K.J., Salunke, D.M.: Structurefunction analysis of tritrypticin, an antibacterial peptide of innate immune origin. J. Biol. Chem. 274, 23296-23304 (1999)
    • (1999) J. Biol. Chem. , vol.274 , pp. 23296-23304
    • Nagpal, S.1    Gupta, V.2    Kaur, K.J.3    Salunke, D.M.4
  • 50
    • 0021170801 scopus 로고
    • Use of the fluorescent probe 1-N-phenylnaphthylamine to study the interactions of aminoglycoside antibiotics with the outer membrane of Pseudomonas aeruginosa
    • Loh, B., Grant, G., Hancock, R.E.W.: Use of the fluorescent probe 1-N-phenylnaphthylamine to study the interactions of aminoglycoside antibiotics with the outer membrane of Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 26, 546-551 (1984)
    • (1984) Antimicrob. Agents Chemother. , vol.26 , pp. 546-551
    • Loh, B.1    Grant, G.2    Hancock, R.E.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.