메뉴 건너뛰기




Volumn 95, Issue , 2015, Pages 63-67

Physical methods to quantify small antibiotic molecules uptake into Gram-negative bacteria

Author keywords

Antibiotics; Flux; Kinetics; Molecular modelling; Porins

Indexed keywords

ANTIBIOTIC AGENT; MEMBRANE PROTEIN; ANTIINFECTIVE AGENT; LIPOPOLYSACCHARIDE; PORIN;

EID: 84944278239     PISSN: 09396411     EISSN: 18733441     Source Type: Journal    
DOI: 10.1016/j.ejpb.2015.05.006     Document Type: Article
Times cited : (41)

References (35)
  • 1
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of bacterial outer membrane permeability revisited
    • H. Nikaido Molecular basis of bacterial outer membrane permeability revisited Microbiol. Mol. Biol. Rev. 67 2003 593 656
    • (2003) Microbiol. Mol. Biol. Rev. , vol.67 , pp. 593-656
    • Nikaido, H.1
  • 2
    • 56349139534 scopus 로고    scopus 로고
    • The porin and the permeating antibiotic: A selective diffusion barrier in Gram-negative bacteria
    • J.M. Pagès, C.E. James, and M. Winterhalter The porin and the permeating antibiotic: a selective diffusion barrier in Gram-negative bacteria Nature Rev. Microbiol. 6 2008 893 903
    • (2008) Nature Rev. Microbiol. , vol.6 , pp. 893-903
    • Pagès, J.M.1    James, C.E.2    Winterhalter, M.3
  • 4
    • 84918539871 scopus 로고    scopus 로고
    • Trends and exception of physical properties on antibacterial activity for Gram-positive and Gram-negative Pathogens
    • D.G. Brown, T.L. May-Dracka, M.M. Gagnon, and R. Tommasi Trends and exception of physical properties on antibacterial activity for Gram-positive and Gram-negative Pathogens J. Med. Chem. 57 2014 10144 10161
    • (2014) J. Med. Chem. , vol.57 , pp. 10144-10161
    • Brown, D.G.1    May-Dracka, T.L.2    Gagnon, M.M.3    Tommasi, R.4
  • 5
    • 84876080238 scopus 로고    scopus 로고
    • Structure, function and regulation of outer membrane proteins involved in drug transport in enterobactericeae: The OmpF/C - TolC Case
    • M. Masi, and J.M. Pagès Structure, function and regulation of outer membrane proteins involved in drug transport in enterobactericeae: the OmpF/C - TolC Case Open Microbiol. J. 7 2013 22 33
    • (2013) Open Microbiol. J. , vol.7 , pp. 22-33
    • Masi, M.1    Pagès, J.M.2
  • 6
    • 84899087499 scopus 로고    scopus 로고
    • TRANSLOCATION project: How to get good drugs into bad bugs
    • R.A. Stavenger, and M. Winterhalter TRANSLOCATION project: how to get good drugs into bad bugs Sci. Transl. Med. 6 2014 228ed7
    • (2014) Sci. Transl. Med. , vol.6 , pp. 228ed7
    • Stavenger, R.A.1    Winterhalter, M.2
  • 7
    • 0033978873 scopus 로고    scopus 로고
    • Substitutions in the eyelet region disrupt cefepime diffusion through the Escherichia coli OmpF channel
    • V. Simonet, M. Malléa, and J.M. Pagès Substitutions in the eyelet region disrupt cefepime diffusion through the Escherichia coli OmpF channel Antimicrob. Agents Chemother. 44 2000 311 315
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 311-315
    • Simonet, V.1    Malléa, M.2    Pagès, J.M.3
  • 9
    • 84872850695 scopus 로고    scopus 로고
    • MG, Siderophore conjugates
    • M.G. Page MG, Siderophore conjugates Ann. N.Y. Acad. Sci. 1277 2013 115 126
    • (2013) Ann. N.Y. Acad. Sci. , vol.1277 , pp. 115-126
    • Page, M.G.1
  • 10
    • 0017703597 scopus 로고
    • Periplasmic space in Salmonella typhimurium and Escherichia coli
    • J.B. Stock, B. Rauch, and S. Roseman Periplasmic space in Salmonella typhimurium and Escherichia coli J. Biol. Chem. 252 1977 7850 7861
    • (1977) J. Biol. Chem. , vol.252 , pp. 7850-7861
    • Stock, J.B.1    Rauch, B.2    Roseman, S.3
  • 11
    • 0026001166 scopus 로고
    • A comparison of methods used for measuring the accumulation of quinolones by Enterobacteriaceae, Pseudomonas Aeruginosa and Staphylococcus aureus
    • P.G. Mortimer, and L.J. Piddock A comparison of methods used for measuring the accumulation of quinolones by Enterobacteriaceae, Pseudomonas Aeruginosa and Staphylococcus aureus J. Antimicrob. Chemother. 38 1991 639 653
    • (1991) J. Antimicrob. Chemother. , vol.38 , pp. 639-653
    • Mortimer, P.G.1    Piddock, L.J.2
  • 12
    • 58149374386 scopus 로고    scopus 로고
    • Development of a liquid chromatography/mass spectrometry-based drug accumulation assay in Pseudomonas aeruginosa
    • H. Cai, K. Rose, L.H. Liang, S. Dunham, and C. Stover Development of a liquid chromatography/mass spectrometry-based drug accumulation assay in Pseudomonas aeruginosa Anal. Biochem. 385 2009 321 325
    • (2009) Anal. Biochem. , vol.385 , pp. 321-325
    • Cai, H.1    Rose, K.2    Liang, L.H.3    Dunham, S.4    Stover, C.5
  • 13
    • 84914142159 scopus 로고    scopus 로고
    • General platform for systematic quantitative evaluation of small molecule permeability in bacteria
    • T.D. Davis, C.J. Gerry, and D.S. Tan General platform for systematic quantitative evaluation of small molecule permeability in bacteria ACS Chem. Biol. 2014
    • (2014) ACS Chem. Biol.
    • Davis, T.D.1    Gerry, C.J.2    Tan, D.S.3
  • 14
    • 84926648408 scopus 로고    scopus 로고
    • Thinking outside the "bug": A unique assay to measure intracellular drug penetration in Gram-negative bacteria
    • Y. Zhou, C. Joubran, L. Miller-Vedam, V. Isabella, A. Nayar, S. Tentarelli, and A. Miller Thinking outside the "bug": a unique assay to measure intracellular drug penetration in Gram-negative bacteria Anal. Chem. 87 2015 3579 3584
    • (2015) Anal. Chem. , vol.87 , pp. 3579-3584
    • Zhou, Y.1    Joubran, C.2    Miller-Vedam, L.3    Isabella, V.4    Nayar, A.5    Tentarelli, S.6    Miller, A.7
  • 15
    • 0017662421 scopus 로고
    • Function of the outer membrane of E coli as a permeability barrier to beta-lactam antibiotics
    • W. Zimmermann, and A. Rosselet Function of the outer membrane of E. coli as a permeability barrier to beta-lactam antibiotics Antimicrobial. Agent Chemoth. 12 1977 368 372
    • (1977) Antimicrobial. Agent Chemoth. , vol.12 , pp. 368-372
    • Zimmermann, W.1    Rosselet, A.2
  • 17
    • 0035856733 scopus 로고    scopus 로고
    • Controlled membrane permeability using bacterial porins. Application to encapsulated enzymes
    • M. Winterhalter, C. Hilty, S.M. Bezrukov, C. Nardin, W. Meier, and D. Fournier Controlled membrane permeability using bacterial porins. Application to encapsulated enzymes Talanta 55 2001 965
    • (2001) Talanta , vol.55 , pp. 965
    • Winterhalter, M.1    Hilty, C.2    Bezrukov, S.M.3    Nardin, C.4    Meier, W.5    Fournier, D.6
  • 18
    • 84862234673 scopus 로고    scopus 로고
    • Antibiotic transport in resistant bacteria: Synchrotron UV fluorescence microscopy to determine antibiotic accumulation with single cell resolution
    • S. Kaščáková, L. Maigre, J. Chevalier, M. Réfrégiers, and J.M. Pagès Antibiotic transport in resistant bacteria: synchrotron UV fluorescence microscopy to determine antibiotic accumulation with single cell resolution PLoS ONE 7 2012 e38624
    • (2012) PLoS ONE , vol.7 , pp. e38624
    • Kaščáková, S.1    Maigre, L.2    Chevalier, J.3    Réfrégiers, M.4    Pagès, J.M.5
  • 19
    • 0018824608 scopus 로고
    • Diffusion of solutes through channels produced by phage lambda receptor protein of Escherichia coli: Inhibition by higher oligosaccharides of maltose series
    • M. Luckey, and H. Nikaido Diffusion of solutes through channels produced by phage lambda receptor protein of Escherichia coli: inhibition by higher oligosaccharides of maltose series Biochem. Biophys. Res. Commun. 93 1980 166 171
    • (1980) Biochem. Biophys. Res. Commun. , vol.93 , pp. 166-171
    • Luckey, M.1    Nikaido, H.2
  • 21
    • 84859962388 scopus 로고    scopus 로고
    • Antibiotic permeation across the OmpF channel: Modulation of the affinity site in the presence of magnesium
    • P.R. Singh, M. Ceccarelli, M. Lovelle, M. Winterhalter, and K.R. Mahendran Antibiotic permeation across the OmpF channel: modulation of the affinity site in the presence of magnesium J. Phys. Chem. B 116 2012 4433 4438
    • (2012) J. Phys. Chem. B , vol.116 , pp. 4433-4438
    • Singh, P.R.1    Ceccarelli, M.2    Lovelle, M.3    Winterhalter, M.4    Mahendran, K.R.5
  • 22
    • 0038637764 scopus 로고    scopus 로고
    • On translocation through a membrane channel via an internal binding site: Kinetics and voltage dependence
    • G. Schwarz, C. Danelon, and M. Winterhalter On translocation through a membrane channel via an internal binding site: kinetics and voltage dependence Biophys. J. 84 2003 2990 2998
    • (2003) Biophys. J. , vol.84 , pp. 2990-2998
    • Schwarz, G.1    Danelon, C.2    Winterhalter, M.3
  • 23
    • 77951100110 scopus 로고    scopus 로고
    • Molecular basis of enrofloxacin translocation through a bacterial porin - When binding does not imply translocation
    • K. Mahendran, and et al. Molecular basis of enrofloxacin translocation through a bacterial porin - when binding does not imply translocation J. Phys. Chem. B 114 2010 5170 5179
    • (2010) J. Phys. Chem. B , vol.114 , pp. 5170-5179
    • Mahendran, K.1
  • 24
    • 84919338453 scopus 로고    scopus 로고
    • Transport across the outer membrane porin of mycolic acid containing actinomycetales: Nocardia farcinica
    • P.R. Singh, H. Bajaj, R. Benz, M. Winterhalter, and R.M. Kozhinjampara Transport across the outer membrane porin of mycolic acid containing actinomycetales: Nocardia farcinica Biochim Biophys. Acta 1847 2014 654 661
    • (2014) Biochim Biophys. Acta , vol.1847 , pp. 654-661
    • Singh, P.R.1    Bajaj, H.2    Benz, R.3    Winterhalter, M.4    Kozhinjampara, R.M.5
  • 25
    • 80051655165 scopus 로고    scopus 로고
    • Simple reconstitution of protein pores in nano lipid bilayers
    • J.L. Gornall, and et al. Simple reconstitution of protein pores in nano lipid bilayers Nano Lett. 11 2011 3334 3340
    • (2011) Nano Lett. , vol.11 , pp. 3334-3340
    • Gornall, J.L.1
  • 26
    • 84934324287 scopus 로고    scopus 로고
    • Analysis of fast channel blockage: Revealing substrate binding in the microsecond range
    • I. Bodrenko, H. Bajaj, P. Ruggerone, M. Winterhalter, and M. Ceccarelli Analysis of fast channel blockage: revealing substrate binding in the microsecond range Analyst 2015 10.1039/C4AN02293A
    • (2015) Analyst
    • Bodrenko, I.1    Bajaj, H.2    Ruggerone, P.3    Winterhalter, M.4    Ceccarelli, M.5
  • 27
    • 0001122076 scopus 로고    scopus 로고
    • Simulation of a protein crystal at constant pressure
    • M. Ceccarelli, and M. Marchi Simulation of a protein crystal at constant pressure J. Phys. Chem. B 101 1998 2105 2108
    • (1998) J. Phys. Chem. B , vol.101 , pp. 2105-2108
    • Ceccarelli, M.1    Marchi, M.2
  • 28
    • 70350035648 scopus 로고    scopus 로고
    • Understanding ion conductance on a molecular level: An all-atom modeling of the bacterial porin OmpF
    • S. Pezeshki, C. Chimerel, A.N. Bessonov, M. Winterhalter, and U. Kleinekathöfer Understanding ion conductance on a molecular level: an all-atom modeling of the bacterial porin OmpF Biophys. J. 97 2009 1898 1906
    • (2009) Biophys. J. , vol.97 , pp. 1898-1906
    • Pezeshki, S.1    Chimerel, C.2    Bessonov, A.N.3    Winterhalter, M.4    Kleinekathöfer, U.5
  • 29
    • 38849122815 scopus 로고    scopus 로고
    • Biased molecular simulations for free-energy mapping: A comparison on the KcsA channel as a test case
    • E. Piccinini, M. Ceccarelli, F. Affinito, R. Brunetti, and C. Jacoboni Biased molecular simulations for free-energy mapping: a comparison on the KcsA channel as a test case J. Chem. Theory Comput. 4 2008 173 183
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 173-183
    • Piccinini, E.1    Ceccarelli, M.2    Affinito, F.3    Brunetti, R.4    Jacoboni, C.5
  • 30
    • 77954911184 scopus 로고    scopus 로고
    • Molecular simulations reveal the mechanism and the determinants for ampicillin translocation through OmpF
    • A. Kumar, E. Hajjar, P. Ruggerone, and M. Ceccarelli Molecular simulations reveal the mechanism and the determinants for ampicillin translocation through OmpF J. Phys. Chem. B 114 2010 9608 9616
    • (2010) J. Phys. Chem. B , vol.114 , pp. 9608-9616
    • Kumar, A.1    Hajjar, E.2    Ruggerone, P.3    Ceccarelli, M.4
  • 31
    • 34648813938 scopus 로고    scopus 로고
    • Diffusion model of solute dynamics in a membrane channel: Mapping onto the two-site model and optimizing the flux
    • S.M. Bezrukov, A.M. Berezhkovskii, and A. Szabo Diffusion model of solute dynamics in a membrane channel: mapping onto the two-site model and optimizing the flux J. Chem. Phys. 127 2007 115101
    • (2007) J. Chem. Phys. , vol.127 , pp. 115101
    • Bezrukov, S.M.1    Berezhkovskii, A.M.2    Szabo, A.3
  • 32
    • 0023472905 scopus 로고
    • Mechanism of sugar transport through the sugar-specific LamB channel of Escherichia coli outer membrane
    • R. Benz, A. Schmid, and G.H. Vos-Scheperkeuter Mechanism of sugar transport through the sugar-specific LamB channel of Escherichia Coli outer membrane J. Membr. Biol. 100 1987 21 29
    • (1987) J. Membr. Biol. , vol.100 , pp. 21-29
    • Benz, R.1    Schmid, A.2    Vos-Scheperkeuter, G.H.3
  • 33
    • 84872600203 scopus 로고    scopus 로고
    • The translocation kinetics of antibiotics through porin OmpC: Insights from structure-based solvation mapping using WaterMap
    • Q.T. Tran, S. Williams, R. Farid, G. Erdemli, and R. Pearlstein The translocation kinetics of antibiotics through porin OmpC: insights from structure-based solvation mapping using WaterMap Proteins 81 2012 291 299
    • (2012) Proteins , vol.81 , pp. 291-299
    • Tran, Q.T.1    Williams, S.2    Farid, R.3    Erdemli, G.4    Pearlstein, R.5
  • 35
    • 84905400486 scopus 로고    scopus 로고
    • Charged residues distribution modulates selectivity of the open state of human isoforms of the voltage dependent anion-selective channel
    • G.F. Amodeo, M.A. Scorciapino, A. Messina, V. De Pinto, and M. Ceccarelli Charged residues distribution modulates selectivity of the open state of human isoforms of the voltage dependent anion-selective channel PLoS ONE 9 2014 e103879
    • (2014) PLoS ONE , vol.9 , pp. e103879
    • Amodeo, G.F.1    Scorciapino, M.A.2    Messina, A.3    De Pinto, V.4    Ceccarelli, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.