메뉴 건너뛰기




Volumn 152, Issue 1-3, 2010, Pages 145-152

Analysis of membrane interactions of antibiotic peptides using ITC and biosensor measurements

Author keywords

Antibiotics; Gallidermin; Isothermal titration calorimetry (ITC); Lipid II; Surface acoustic wave (SAW) biosensor; Vancomycin

Indexed keywords

DIPALMITOYLPHOSPHATIDYLCHOLINE; GALLIDERMIN; LIPID; POLYPEPTIDE ANTIBIOTIC AGENT; VANCOMYCIN;

EID: 78149284424     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2010.09.002     Document Type: Article
Times cited : (21)

References (39)
  • 1
    • 0036948138 scopus 로고    scopus 로고
    • Mode of action of membrane active antimicrobial peptides
    • Shai Y. Mode of action of membrane active antimicrobial peptides. Biopolymers 2002, 66:236-248.
    • (2002) Biopolymers , vol.66 , pp. 236-248
    • Shai, Y.1
  • 2
    • 16844362681 scopus 로고    scopus 로고
    • Molecular mechanisms of membrane perturbation by antimicrobial peptides and the use of biophysical studies in the design of novel peptide antibiotics
    • Lohner K., Blondelle S.E. Molecular mechanisms of membrane perturbation by antimicrobial peptides and the use of biophysical studies in the design of novel peptide antibiotics. Comb. Chem. High Throughput Screen. 2005, 8:241-256.
    • (2005) Comb. Chem. High Throughput Screen. , vol.8 , pp. 241-256
    • Lohner, K.1    Blondelle, S.E.2
  • 3
    • 0014013113 scopus 로고
    • Compounds formed between nucleotides related to the biosynthesis of bacterial cell wall and vancomycin
    • Chatterjee A.N., Perkins H.R. Compounds formed between nucleotides related to the biosynthesis of bacterial cell wall and vancomycin. Biochem. Biophys. Res. Commun. 1966, 24:489-494.
    • (1966) Biochem. Biophys. Res. Commun. , vol.24 , pp. 489-494
    • Chatterjee, A.N.1    Perkins, H.R.2
  • 4
    • 0032226551 scopus 로고    scopus 로고
    • Peptidoglycan biosynthesis. Unexploited antibacterial targets within a familiar pathway
    • Wong K.K., Pompliano D.L. Peptidoglycan biosynthesis. Unexploited antibacterial targets within a familiar pathway. Adv. Exp. Med. Biol. 1998, 456:197-217.
    • (1998) Adv. Exp. Med. Biol. , vol.456 , pp. 197-217
    • Wong, K.K.1    Pompliano, D.L.2
  • 7
    • 0031784281 scopus 로고    scopus 로고
    • Role of lipid-bound peptidoglycan precursors in the formation of pores by nisin, epidermin and other lantibiotics
    • Brötz H., Josten M., Wiedemann I., Schneider U., Götz F., Bierbaum G., et al. Role of lipid-bound peptidoglycan precursors in the formation of pores by nisin, epidermin and other lantibiotics. Mol. Microbiol. 1998, 30:317-327.
    • (1998) Mol. Microbiol. , vol.30 , pp. 317-327
    • Brötz, H.1    Josten, M.2    Wiedemann, I.3    Schneider, U.4    Götz, F.5    Bierbaum, G.6
  • 8
    • 4444277132 scopus 로고    scopus 로고
    • Assembly and stability of nisin-lipid II pores
    • Hasper H.E., de Kruijff B., Breukink E. Assembly and stability of nisin-lipid II pores. Biochemistry 2004, 43:11567-11575.
    • (2004) Biochemistry , vol.43 , pp. 11567-11575
    • Hasper, H.E.1    de Kruijff, B.2    Breukink, E.3
  • 10
    • 0037044318 scopus 로고    scopus 로고
    • Lipid II induces a transmembrane orientation of the pore-forming peptide lantibiotic nisin
    • van Heusden H.E., de Kruijff B., Breukink E. Lipid II induces a transmembrane orientation of the pore-forming peptide lantibiotic nisin. Biochemistry 2002, 41:12171-12178.
    • (2002) Biochemistry , vol.41 , pp. 12171-12178
    • van Heusden, H.E.1    de Kruijff, B.2    Breukink, E.3
  • 12
    • 33645779735 scopus 로고    scopus 로고
    • Insights into in vivo activities of lantibiotics from gallidermin and epidermin mode-of-action studies
    • Bonelli R.R., Schneider T., Sahl H., Wiedemann I. Insights into in vivo activities of lantibiotics from gallidermin and epidermin mode-of-action studies. Antimicrob. Agents Chemother. 2006, 50:1449-1457.
    • (2006) Antimicrob. Agents Chemother. , vol.50 , pp. 1449-1457
    • Bonelli, R.R.1    Schneider, T.2    Sahl, H.3    Wiedemann, I.4
  • 13
    • 0017802490 scopus 로고
    • Structure of vancomycin and its complex with acetyl-d-alanyl-d-alanine
    • Sheldrick G.M., Jones P.G., Kennard O., Williams D.H., Smith G.A. Structure of vancomycin and its complex with acetyl-d-alanyl-d-alanine. Nature 1978, 271:223-225.
    • (1978) Nature , vol.271 , pp. 223-225
    • Sheldrick, G.M.1    Jones, P.G.2    Kennard, O.3    Williams, D.H.4    Smith, G.A.5
  • 14
    • 34047151952 scopus 로고    scopus 로고
    • Single-molecule force spectroscopy and imaging of the vancomycin/D-Ala-D-Ala interaction
    • Gilbert Y., Deghorain M., Wang L., Xu B., Pollheimer P.D., Gruber H.J., et al. Single-molecule force spectroscopy and imaging of the vancomycin/D-Ala-D-Ala interaction. Nano Lett. 2007, 7:796-801.
    • (2007) Nano Lett. , vol.7 , pp. 796-801
    • Gilbert, Y.1    Deghorain, M.2    Wang, L.3    Xu, B.4    Pollheimer, P.D.5    Gruber, H.J.6
  • 16
    • 0031627006 scopus 로고    scopus 로고
    • Microcalorimetry of protein-protein interactions
    • Cooper A. Microcalorimetry of protein-protein interactions. Methods Mol. Biol. 1998, 88:11-22.
    • (1998) Methods Mol. Biol. , vol.88 , pp. 11-22
    • Cooper, A.1
  • 17
    • 0034953839 scopus 로고    scopus 로고
    • Making cool drugs hot: isothermal titration calorimetry as a tool to study binding energetics
    • 168, 170 passim
    • Holdgate G.A. Making cool drugs hot: isothermal titration calorimetry as a tool to study binding energetics. Biotechniques 2001, 31:164-166. 168, 170 passim.
    • (2001) Biotechniques , vol.31 , pp. 164-166
    • Holdgate, G.A.1
  • 18
    • 0041843710 scopus 로고    scopus 로고
    • Charge-dependent translocation of the Trojan peptide penetratin across lipid membranes
    • Binder H., Lindblom G. Charge-dependent translocation of the Trojan peptide penetratin across lipid membranes. Biophys. J. 2003, 85:982-995.
    • (2003) Biophys. J. , vol.85 , pp. 982-995
    • Binder, H.1    Lindblom, G.2
  • 19
    • 0032539980 scopus 로고    scopus 로고
    • Magainin 2 amide interaction with lipid membranes: calorimetric detection of peptide binding and pore formation
    • Wenk M.R., Seelig J. Magainin 2 amide interaction with lipid membranes: calorimetric detection of peptide binding and pore formation. Biochemistry 1998, 37:3909-3916.
    • (1998) Biochemistry , vol.37 , pp. 3909-3916
    • Wenk, M.R.1    Seelig, J.2
  • 20
    • 33745410738 scopus 로고    scopus 로고
    • Thermodynamics of interactions of vancomycin and synthetic surrogates of bacterial cell wall
    • Rekharsky M., Hesek D., Lee M., Meroueh S.O., Inoue Y., Mobashery S. Thermodynamics of interactions of vancomycin and synthetic surrogates of bacterial cell wall. J. Am. Chem. Soc. 2006, 128:7736-7737.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 7736-7737
    • Rekharsky, M.1    Hesek, D.2    Lee, M.3    Meroueh, S.O.4    Inoue, Y.5    Mobashery, S.6
  • 21
    • 0034702860 scopus 로고    scopus 로고
    • Binding of Nisin Z to bilayer vesicles as determined with isothermal titration calorimetry
    • Breukink E., Ganz P., de Kruijff B., Seelig J. Binding of Nisin Z to bilayer vesicles as determined with isothermal titration calorimetry. Biochemistry 2000, 39:10247-10254.
    • (2000) Biochemistry , vol.39 , pp. 10247-10254
    • Breukink, E.1    Ganz, P.2    de Kruijff, B.3    Seelig, J.4
  • 22
    • 0030969611 scopus 로고    scopus 로고
    • The lantibiotic mersacidin inhibits peptidoglycan biosynthesis at the level of transglycosylation
    • Brötz H., Bierbaum G., Reynolds P.E., Sahl H.G. The lantibiotic mersacidin inhibits peptidoglycan biosynthesis at the level of transglycosylation. Eur. J. Biochem. 1997, 246:193-199.
    • (1997) Eur. J. Biochem. , vol.246 , pp. 193-199
    • Brötz, H.1    Bierbaum, G.2    Reynolds, P.E.3    Sahl, H.G.4
  • 23
    • 3242890388 scopus 로고    scopus 로고
    • In vitro assembly of a complete, pentaglycine interpeptide bridge containing cell wall precursor (lipid II-Gly5) of Staphylococcus aureus
    • Schneider T., Senn M.M., Berger-Bächi B., Tossi A., Sahl H., Wiedemann I. In vitro assembly of a complete, pentaglycine interpeptide bridge containing cell wall precursor (lipid II-Gly5) of Staphylococcus aureus. Mol. Microbiol. 2004, 53:675-685.
    • (2004) Mol. Microbiol. , vol.53 , pp. 675-685
    • Schneider, T.1    Senn, M.M.2    Berger-Bächi, B.3    Tossi, A.4    Sahl, H.5    Wiedemann, I.6
  • 24
    • 29844445436 scopus 로고    scopus 로고
    • The detection of UV-induced membrane damages by a combination of two biosensor techniques
    • Christ K., Rüttinger H., Höpfner M., Rothe U., Bendas G. The detection of UV-induced membrane damages by a combination of two biosensor techniques. Photochem. Photobiol. 2005, 81:1417-1423.
    • (2005) Photochem. Photobiol. , vol.81 , pp. 1417-1423
    • Christ, K.1    Rüttinger, H.2    Höpfner, M.3    Rothe, U.4    Bendas, G.5
  • 25
    • 33847081264 scopus 로고    scopus 로고
    • The role of lipid II in membrane binding of and pore formation by nisin analyzed by two combined biosensor techniques
    • Christ K., Wiedemann I., Bakowsky U., Sahl H., Bendas G. The role of lipid II in membrane binding of and pore formation by nisin analyzed by two combined biosensor techniques. Biochim. Biophys. Acta 2007, 1768:694-704.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 694-704
    • Christ, K.1    Wiedemann, I.2    Bakowsky, U.3    Sahl, H.4    Bendas, G.5
  • 26
    • 0001457369 scopus 로고
    • The role of polyamines in the neutralization of bacteriophage deoxyribonucleic acid
    • Ames B., Dubin D. The role of polyamines in the neutralization of bacteriophage deoxyribonucleic acid. J. Biol. Chem. 1960, 235:769-775.
    • (1960) J. Biol. Chem. , vol.235 , pp. 769-775
    • Ames, B.1    Dubin, D.2
  • 30
    • 0021993065 scopus 로고
    • Mode of action of the peptide antibiotic nisin and influence on the membrane potential of whole cells and on cytoplasmic and artificial membrane vesicles
    • Ruhr E., Sahl H.G. Mode of action of the peptide antibiotic nisin and influence on the membrane potential of whole cells and on cytoplasmic and artificial membrane vesicles. Antimicrob. Agents Chemother. 1985, 27:841-845.
    • (1985) Antimicrob. Agents Chemother. , vol.27 , pp. 841-845
    • Ruhr, E.1    Sahl, H.G.2
  • 31
    • 67649624728 scopus 로고    scopus 로고
    • Influence of Ca(2+) ions on the activity of lantibiotics containing a mersacidin-like lipid II binding motif
    • Böttiger T., Schneider T., Martínez B., Sahl H., Wiedemann I. Influence of Ca(2+) ions on the activity of lantibiotics containing a mersacidin-like lipid II binding motif. Appl. Environ. Microbiol. 2009, 75:4427-4434.
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 4427-4434
    • Böttiger, T.1    Schneider, T.2    Martínez, B.3    Sahl, H.4    Wiedemann, I.5
  • 32
    • 34548741226 scopus 로고    scopus 로고
    • Synthesis of bicyclic alkene-/alkane-bridged nisin mimics by ring-closing metathesis and their biochemical evaluation as lipid II binders: toward the design of potential novel antibiotics
    • Ghalit N., Reichwein J.F., Hilbers H.W., Breukink E., Rijkers D.T.S., Liskamp R.M.J. Synthesis of bicyclic alkene-/alkane-bridged nisin mimics by ring-closing metathesis and their biochemical evaluation as lipid II binders: toward the design of potential novel antibiotics. Chembiochem 2007, 8:1540-1554.
    • (2007) Chembiochem , vol.8 , pp. 1540-1554
    • Ghalit, N.1    Reichwein, J.F.2    Hilbers, H.W.3    Breukink, E.4    Rijkers, D.T.S.5    Liskamp, R.M.J.6
  • 33
    • 38349093526 scopus 로고    scopus 로고
    • An electrochemical study into the interaction between complement-derived peptides and DOPC mono- and bilayers
    • Ringstad L., Protopapa E., Lindholm-Sethson B., Schmidtchen A., Nelson A., Malmsten M. An electrochemical study into the interaction between complement-derived peptides and DOPC mono- and bilayers. Langmuir 2008, 24:208-216.
    • (2008) Langmuir , vol.24 , pp. 208-216
    • Ringstad, L.1    Protopapa, E.2    Lindholm-Sethson, B.3    Schmidtchen, A.4    Nelson, A.5    Malmsten, M.6
  • 34
    • 0028942365 scopus 로고
    • Dimerization and membrane anchors in extracellular targeting of vancomycin group antibiotics
    • Beauregard D.A., Williams D.H., Gwynn M.N., Knowles D.J. Dimerization and membrane anchors in extracellular targeting of vancomycin group antibiotics. Antimicrob. Agents Chemother. 1995, 39:781-785.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 781-785
    • Beauregard, D.A.1    Williams, D.H.2    Gwynn, M.N.3    Knowles, D.J.4
  • 35
    • 68949173708 scopus 로고    scopus 로고
    • Interactions of oritavancin, a new lipoglycopeptide derived from vancomycin, with phospholipid bilayers: effect on membrane permeability and nanoscale lipid membrane organization
    • Domenech O., Francius G., Tulkens P.M., Van Bambeke F., Dufrêne Y., Mingeot-Leclercq M. Interactions of oritavancin, a new lipoglycopeptide derived from vancomycin, with phospholipid bilayers: effect on membrane permeability and nanoscale lipid membrane organization. Biochim. Biophys. Acta 2009, 1788:1832-1840.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1832-1840
    • Domenech, O.1    Francius, G.2    Tulkens, P.M.3    Van Bambeke, F.4    Dufrêne, Y.5    Mingeot-Leclercq, M.6
  • 36
    • 50849097211 scopus 로고    scopus 로고
    • Surface acoustic wave biosensor as a tool to study the interaction of antimicrobial peptides with phospholipid and lipopolysaccharide model membranes
    • Andrä J., Böhling A., Gronewold T.M.A., Schlecht U., Perpeet M., Gutsmann T. Surface acoustic wave biosensor as a tool to study the interaction of antimicrobial peptides with phospholipid and lipopolysaccharide model membranes. Langmuir 2008, 24:9148-9153.
    • (2008) Langmuir , vol.24 , pp. 9148-9153
    • Andrä, J.1    Böhling, A.2    Gronewold, T.M.A.3    Schlecht, U.4    Perpeet, M.5    Gutsmann, T.6
  • 37
    • 0031567121 scopus 로고    scopus 로고
    • Titration calorimetry of lipid-peptide interactions
    • Seelig J. Titration calorimetry of lipid-peptide interactions. Biochim. Biophys. Acta 1997, 1331:103-116.
    • (1997) Biochim. Biophys. Acta , vol.1331 , pp. 103-116
    • Seelig, J.1
  • 38
    • 0021113818 scopus 로고
    • Merocyanine 540, a fluorescent probe sensitive to lipid packing
    • Williamson P., Mattocks K., Schlegel R.A. Merocyanine 540, a fluorescent probe sensitive to lipid packing. Biochim. Biophys. Acta 1983, 732:387-393.
    • (1983) Biochim. Biophys. Acta , vol.732 , pp. 387-393
    • Williamson, P.1    Mattocks, K.2    Schlegel, R.A.3
  • 39
    • 33748766086 scopus 로고    scopus 로고
    • An alternative bactericidal mechanism of action for lantibiotic peptides that target lipid II
    • Hasper H.E., Kramer N.E., Smith J.L., Hillman J.D., Zachariah C., Kuipers O.P., et al. An alternative bactericidal mechanism of action for lantibiotic peptides that target lipid II. Science 2006, 313:1636-1637.
    • (2006) Science , vol.313 , pp. 1636-1637
    • Hasper, H.E.1    Kramer, N.E.2    Smith, J.L.3    Hillman, J.D.4    Zachariah, C.5    Kuipers, O.P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.