Login Register Cart 0
General Review Article

针对细菌细胞壁的抗菌剂

卷 27, 期 17, 2020

页: [2902 - 2926] 页: 25

弟呕挨: 10.2174/0929867327666200128103653

价格: $65

摘要

抗生素通过杀死或抑制细菌的生长来治疗细菌感染，与此同时，人们也在研究抗生素杀死细菌或抑制细菌增殖的机制。在这种情况下，活性在细菌细胞壁上的抗菌剂的出现，对于对抗引起严重疾病的细菌制剂具有根本的重要性。事实上，细胞壁在生命周期中起着许多作用，是大多数细菌的基本组成部分。本文主要介绍肽聚糖生物合成的胞内步骤，以及基于参与这些细胞膜成分形成早期步骤的酶的新型抗菌药物的研究。

关键词: 抗生素，细菌细胞壁，肽聚糖，酵素，综述，细菌感染。

« Previous Next »
[1]
Vollmer, W.; Blanot, D.; de Pedro, M.A. Peptidoglycan structure and architecture. FEMS Microbiol. Rev., 2008, 32(2), 149-167.
[http://dx.doi.org/10.1111/j.1574-6976.2007.00094.x] [PMID: 18194336]
[2]
Typas, A.; Banzhaf, M.; Gross, C.A.; Vollmer, W. From the regulation of peptidoglycan synthesis to bacterial growth and morphology. Nat. Rev. Microbiol., 2011, 10(2), 123-136.
[http://dx.doi.org/10.1038/nrmicro2677] [PMID: 22203377]
[3]
Zapun, A.; Philippe, J.; Abrahams, K.A.; Signor, L.; Roper, D.I.; Breukink, E.; Vernet, T. In vitro reconstitution of peptidoglycan assembly from the Gram-positive pathogen Streptococcus pneumoniae. ACS Chem. Biol., 2013, 8(12), 2688-2696.
[http://dx.doi.org/10.1021/cb400575t] [PMID: 24044435]
[4]
Mainardi, J-L.; Legrand, R.; Arthur, M.; Schoot, B.; van Heijenoort, J.; Gutmann, L. Novel mechanism of β-lactam resistance due to bypass of DD-transpeptidation in Enterococcus faecium. J. Biol. Chem., 2000, 275(22), 16490-16496.
[http://dx.doi.org/10.1074/jbc.M909877199] [PMID: 10748168]
[5]
Glauner, B.; Höltje, J-V.; Schwarz, U. The composition of the murein of Escherichia coli. J. Biol. Chem., 1988, 263(21), 10088-10095.
[PMID: 3292521]
[6]
Bui, N.K.; Eberhardt, A.; Vollmer, D.; Kern, T.; Bougault, C.; Tomasz, A.; Simorre, J-P.; Vollmer, W. Isolation and analysis of cell wall components from Streptococcus pneumoniae. Anal. Biochem., 2012, 421(2), 657-666.
[http://dx.doi.org/10.1016/j.ab.2011.11.026] [PMID: 22192687]
[7]
Amano, K.; Hayashi, H.; Araki, Y.; Ito, E. The action of lysozyme on peptidoglycan with N-unsubstituted glucosamine residues. Isolation of glycan fragments and their susceptibility to lysozyme. Eur. J. Biochem., 1977, 76(1), 299-307.
[http://dx.doi.org/10.1111/j.1432-1033.1977.tb11596.x] [PMID: 407083]
[8]
Bernard, E.; Rolain, T.; Courtin, P.; Guillot, A.; Langella, P.; Hols, P.; Chapot-Chartier, M.P. Characterization of O-acetylation of N-acetylglucosamine: a novel structural variation of bacterial peptidoglycan. J. Biol. Chem., 2011, 286(27), 23950-23958.
[http://dx.doi.org/10.1074/jbc.M111.241414] [PMID: 21586574]
[9]
Lovering, A.L.; Safadi, S.S.; Strynadka, N.C.J. Structural perspective of peptidoglycan biosynthesis and assembly. Annu. Rev. Biochem., 2012, 81, 451-478.
[http://dx.doi.org/10.1146/annurev-biochem-061809-112742] [PMID: 22663080]
[10]
Chung, B.C.; Zhao, J.; Gillespie, R.A.; Kwon, D-Y.; Guan, Z.; Hong, J.; Zhou, P.; Lee, S-Y. Crystal structure of MraY, an essential membrane enzyme for bacterial cell wall synthesis. Science, 2013, 341(6149), 1012-1016.
[http://dx.doi.org/10.1126/science.1236501] [PMID: 23990562]
[11]
Chang, H-Y.; Chou, C-C.; Hsu, M-F.; Wang, A.H.J. Proposed carrier lipid-binding site of undecaprenyl pyrophosphate phosphatase from Escherichia coli. J. Biol. Chem., 2014, 289(27), 18719-18735.
[http://dx.doi.org/10.1074/jbc.M114.575076] [PMID: 24855653]
[12]
Ishii, K.; Sagami, H.; Ogura, K. A novel prenyltransferase from Paracoccus denitrificans. Biochem. J., 1986, 233(3), 773-777.
[http://dx.doi.org/10.1042/bj2330773] [PMID: 3707524]
[13]
Kaur, D.; Brennan, P.J.; Crick, D.C. Decaprenyl diphosphate synthesis in Mycobacterium tuberculosis. J. Bacteriol., 2004, 186(22), 7564-7570.
[http://dx.doi.org/10.1128/JB.186.22.7564-7570.2004] [PMID: 15516568]
[14]
Hendlin, D.; Stapley, E.O.; Jackson, M.; Wallick, H.; Miller, A.K.; Wolf, F.J.; Miller, T.W.; Chaiet, L.; Kahan, F.M.; Foltz, E.L.; Woodruff, H.B.; Mata, J.M.; Hernandez, S.; Mochales, S. Phosphonomycin, a new antibiotic produced by strains of streptomyces. Science, 1969, 166(3901), 122-123.
[http://dx.doi.org/10.1126/science.166.3901.122] [PMID: 5809587]
[15]
Hrast, M.; Sosič, I.; Šink, R.; Gobec, S. Inhibitors of the peptidoglycan biosynthesis enzymes MurA-F. Bioorg. Chem., 2014, 55, 2-15.
[http://dx.doi.org/10.1016/j.bioorg.2014.03.008] [PMID: 24755374]
[16]
Marquardt, J.L.; Brown, E.D.; Lane, W.S.; Haley, T.M.; Ichikawa, Y.; Wong, C-H.; Walsh, C.T. Kinetics, stoichiometry, and identification of the reactive thiolate in the inactivation of UDP-GlcNAc enolpyruvoyl transferase by the antibiotic fosfomycin. Biochemistry, 1994, 33(35), 10646-10651.
[http://dx.doi.org/10.1021/bi00201a011] [PMID: 8075065]
[17]
Castañeda-García, A.; Blázquez, J.; Rodríguez-Rojas, A. Molecular mechanisms and clinical impact of acquired and intrinsic fosfomycin resistance. Antibiotics (Basel), 2013, 2(2), 217-236.
[http://dx.doi.org/10.3390/antibiotics2020217] [PMID: 27029300]
[18]
Baum, E.Z.; Montenegro, D.A.; Licata, L.; Turchi, I.; Webb, G.C.; Foleno, B.D.; Bush, K. Identification and characterization of new inhibitors of the Escherichia coli MurA enzyme. Antimicrob. Agents Chemother., 2001, 45(11), 3182-3188.
[http://dx.doi.org/10.1128/AAC.45.11.3182-3188.2001] [PMID: 11600375]
[19]
Barbosa, M.D.F.S.; Yang, G.; Fang, J.; Kurilla, M.G.; Pompliano, D.L. Development of a whole-cell assay for peptidoglycan biosynthesis inhibitors. Antimicrob. Agents Chemother., 2002, 46(4), 943-946.
[http://dx.doi.org/10.1128/AAC.46.4.943-946.2002] [PMID: 11897573]
[20]
Eschenburg, S.; Priestman, M.A.; Abdul-Latif, F.A.; Delachaume, C.; Fassy, F.; Schönbrunn, E. A novel inhibitor that suspends the induced fit mechanism of UDP-N-acetylglucosamine enolpyruvyl transferase (MurA). J. Biol. Chem., 2005, 280(14), 14070-14075.
[http://dx.doi.org/10.1074/jbc.M414412200] [PMID: 15701635]
[21]
Bachelier, A.; Mayer, R.; Klein, C.D. Sesquiterpene lactones are potent and irreversible inhibitors of the antibacterial target enzyme MurA. Bioorg. Med. Chem. Lett., 2006, 16(21), 5605-5609.
[http://dx.doi.org/10.1016/j.bmcl.2006.08.021] [PMID: 16945528]
[22]
Steinbach, A.; Scheidig, A.J.; Klein, C.D. The unusual binding mode of cnicin to the antibacterial target enzyme MurA revealed by X-ray crystallography. J. Med. Chem., 2008, 51(16), 5143-5147.
[http://dx.doi.org/10.1021/jm800609p] [PMID: 18672863]
[23]
Mendgen, T.; Scholz, T.; Klein, C.D. Structure-activity relationships of tulipalines, tuliposides, and related compounds as inhibitors of MurA. Bioorg. Med. Chem. Lett., 2010, 20(19), 5757-5762.
[http://dx.doi.org/10.1016/j.bmcl.2010.07.139] [PMID: 20729083]
[24]
Scholz, T.; Heyl, C.L.; Bernardi, D.; Zimmermann, S.; Kattner, L.; Klein, C.D. Chemical, biochemical and microbiological properties of a brominated nitrovinylfuran with broad-spectrum antibacterial activity. Bioorg. Med. Chem., 2013, 21(3), 795-804.
[http://dx.doi.org/10.1016/j.bmc.2012.11.018] [PMID: 23266177]
[25]
Dunsmore, C.J.; Miller, K.; Blake, K.L.; Patching, S.G.; Henderson, P.J.F.; Garnett, J.A.; Stubbings, W.J.; Phillips, S.E.V.; Palestrant, D.J.; Angeles, Jde.L.; Leeds, J.A.; Chopra, I.; Fishwick, C.W. 2-Aminotetralones: novel inhibitors of MurA and MurZ. Bioorg. Med. Chem. Lett., 2008, 18(5), 1730-1734.
[http://dx.doi.org/10.1016/j.bmcl.2008.01.089] [PMID: 18261901]
[26]
Miller, K.; Dunsmore, C.J.; Leeds, J.A.; Patching, S.G.; Sachdeva, M.; Blake, K.L.; Stubbings, W.J.; Simmons, K.J.; Henderson, P.J.F.; De Los Angeles, J.; Fishwick, C.W.G.; Chopra, I. Benzothioxalone derivatives as novel inhibitors of UDP-N-acetylglucosamine enolpyruvyl transferases (MurA and MurZ). J. Antimicrob. Chemother., 2010, 65(12), 2566-2573.
[http://dx.doi.org/10.1093/jac/dkq349] [PMID: 20861142]
[27]
Jin, B-S.; Han, S-G.; Lee, W-K.; Ryoo, S.W.; Lee, S.J.; Suh, S-W.; Yu, Y.G. Inhibitory mechanism of novel inhibitors of UDP-N-acetylglucosamine enolpyruvyl transferase from Haemophilus influenzae. J. Microbiol. Biotechnol., 2009, 19(12), 1582-1589.
[http://dx.doi.org/10.4014/jmb.0905.05036] [PMID: 20075623]
[28]
Han, H.; Yang, Y.; Olesen, S.H.; Becker, A.; Betzi, S.; Schönbrunn, E. The fungal product terreic acid is a covalent inhibitor of the bacterial cell wall biosynthetic enzyme UDP-N-acetylglucosamine 1-carboxyvinyltransferase (MurA). Biochemistry, 2010, 49(19), 4276-4282.
[http://dx.doi.org/10.1021/bi100365b] [PMID: 20392080]
[29]
Sharma, R.; Lambu, M.R.; Jamwal, U.; Rani, C.; Chib, R.; Wazir, P.; Mukherjee, D.; Chaubey, A.; Khan, I.A. Escherichia coli N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) inhibitory activity of terreic acid isolated from Aspergillus terreus. J. Biomol. Screen., 2016, 21(4), 342-353.
[http://dx.doi.org/10.1177/1087057115625308] [PMID: 26762501]
[30]
Chang, C-M.; Chern, J.; Chen, M-Y.; Huang, K-F.; Chen, C-H.; Yang, Y-L.; Wu, S-H. Avenaciolides: potential MurA-targeted inhibitors against peptidoglycan biosynthesis in methicillin-resistant Staphylococcus aureus (MRSA). J. Am. Chem. Soc., 2015, 137(1), 267-275.
[http://dx.doi.org/10.1021/ja510375f] [PMID: 25521652]
[31]
Kumar, A.; Saranathan, R.; Prashanth, K.; Tiwary, B.K.; Krishna, R. Inhibition of the MurA enzyme in Fusobacterium nucleatum by potential inhibitors identified through computational and in vitro approaches. Mol. Biosyst., 2017, 13(5), 939-954.
[http://dx.doi.org/10.1039/C7MB00074J] [PMID: 28358152]
[32]
Benson, T.E.; Walsh, C.T.; Hogle, J.M. The structure of the substrate-free form of MurB, an essential enzyme for the synthesis of bacterial cell walls. Structure, 1996, 4(1), 47-54.
[http://dx.doi.org/10.1016/S0969-2126(96)00008-1] [PMID: 8805513]
[33]
Andres, C.J.; Bronson, J.J.; D’Andrea, S.V.; Deshpande, M.S.; Falk, P.J.; Grant-Young, K.A.; Harte, W.E.; Ho, H-T.; Misco, P.F.; Robertson, J.G.; Stock, D.; Sun, Y.; Walsh, A.W. 4-Thiazolidinones: novel inhibitors of the bacterial enzyme MurB. Bioorg. Med. Chem. Lett., 2000, 10(8), 715-717.
[http://dx.doi.org/10.1016/S0960-894X(00)00073-1] [PMID: 10782671]
[34]
Bronson, J.J.; DenBleyker, K.L.; Falk, P.J.; Mate, R.A.; Ho, H-T.; Pucci, M.J.; Snyder, L.B. Discovery of the first antibacterial small molecule inhibitors of MurB. Bioorg. Med. Chem. Lett., 2003, 13(5), 873-875.
[http://dx.doi.org/10.1016/S0960-894X(02)01076-4] [PMID: 12617911]
[35]
Sarver, R.W.; Rogers, J.M.; Epps, D.E. Determination of ligand-MurB interactions by isothermal denaturation: application as a secondary assay to complement high throughput screening. J. Biomol. Screen., 2002, 7(1), 21-28.
[http://dx.doi.org/10.1089/108705702753520305] [PMID: 11897052]
[36]
Kutterer, K.M.K.; Davis, J.M.; Singh, G.; Yang, Y.; Hu, W.; Severin, A.; Rasmussen, B.A.; Krishnamurthy, G.; Failli, A.; Katz, A.H. 4-Alkyl and 4,4′-dialkyl 1,2-bis(4-chlorophenyl)pyrazolidine-3,5-dione derivatives as new inhibitors of bacterial cell wall biosynthesis. Bioorg. Med. Chem. Lett., 2005, 15(10), 2527-2531.
[http://dx.doi.org/10.1016/j.bmcl.2005.03.058] [PMID: 15863310]
[37]
Yang, Y.; Severin, A.; Chopra, R.; Krishnamurthy, G.; Singh, G.; Hu, W.; Keeney, D.; Svenson, K.; Petersen, P.J.; Labthavikul, P.; Shlaes, D.M.; Rasmussen, B.A.; Failli, A.A.; Shumsky, J.S.; Kutterer, K.M.K.; Gilbert, A.; Mansour, T.S. 3,5-dioxopyrazolidines, novel inhibitors of UDP-N- acetylenolpyruvylglucosamine reductase (MurB) with activity against gram-positive bacteria. Antimicrob. Agents Chemother., 2006, 50(2), 556-564.
[http://dx.doi.org/10.1128/AAC.50.2.556-564.2006] [PMID: 16436710]
[38]
Gilbert, A.M.; Failli, A.; Shumsky, J.; Yang, Y.; Severin, A.; Singh, G.; Hu, W.; Keeney, D.; Petersen, P.J.; Katz, A.H. Pyrazolidine-3,5-diones and 5-hydroxy-1H-pyrazol-3(2H)-ones, inhibitors of UDP-N-acetylenolpyruvyl glucosamine reductase. J. Med. Chem., 2006, 49(20), 6027-6036.
[http://dx.doi.org/10.1021/jm060499t] [PMID: 17004716]
[39]
Francisco, G.D.; Li, Z.; Albright, J.D.; Eudy, N.H.; Katz, A.H.; Petersen, P.J.; Labthavikul, P.; Singh, G.; Yang, Y.; Rasmussen, B.A.; Lin, Y-I.; Mansour, T.S. Phenyl thiazolyl urea and carbamate derivatives as new inhibitors of bacterial cell-wall biosynthesis. Bioorg. Med. Chem. Lett., 2004, 14(1), 235-238.
[http://dx.doi.org/10.1016/j.bmcl.2003.09.082] [PMID: 14684334]
[40]
Mansour, T.S.; Caufield, C.E.; Rasmussen, B.; Chopra, R.; Krishnamurthy, G.; Morris, K.M.; Svenson, K.; Bard, J.; Smeltzer, C.; Naughton, S.; Antane, S.; Yang, Y.; Severin, A.; Quagliato, D.; Petersen, P.J.; Singh, G. Naphthyl tetronic acids as multi-target inhibitors of bacterial peptidoglycan biosynthesis. Chem. Med. Chem, 2007, 2(10), 1414-1417.
[http://dx.doi.org/10.1002/cmdc.200700094] [PMID: 17600795]
[41]
Reck, F.; Marmor, S.; Fisher, S.; Wuonola, M.A. Inhibitors of the bacterial cell wall biosynthesis enzyme MurC. Bioorg. Med. Chem. Lett., 2001, 11(11), 1451-1454.
[http://dx.doi.org/10.1016/S0960-894X(01)00251-7] [PMID: 11378375]
[42]
Marmor, S.; Petersen, C.P.; Reck, F.; Yang, W.; Gao, N.; Fisher, S.L. Biochemical characterization of a phosphinate inhibitor of Escherichia coli MurC. Biochemistry, 2001, 40(40), 12207-12214.
[http://dx.doi.org/10.1021/bi015567m] [PMID: 11580296]
[43]
Sim, M.M.; Ng, S.B.; Buss, A.D.; Crasta, S.C.; Goh, K.L.; Lee, S.K. Benzylidene rhodanines as novel inhibitors of UDP-N-acetylmuramate/L-alanine ligase. Bioorg. Med. Chem. Lett., 2002, 12(4), 697-699.
[http://dx.doi.org/10.1016/S0960-894X(01)00832-0] [PMID: 11844704]
[44]
Foye, W.O.; Tovivich, P. N-Glucopyranosyl-5-aralkylidenerhodanines: synthesis and antibacterial and antiviral activities. J. Pharm. Sci., 1977, 66(11), 1607-1611.
[http://dx.doi.org/10.1002/jps.2600661126] [PMID: 915738]
[45]
Ehmann, D.E.; Demeritt, J.E.; Hull, K.G.; Fisher, S.L. Biochemical characterization of an inhibitor of Escherichia coli UDP-N-acetylmuramyl-l-alanine ligase. Biochim. Biophys. Acta, 2004, 1698(2), 167-174.
[http://dx.doi.org/10.1016/j.bbapap.2003.11.006] [PMID: 15134649]
[46]
Zawadzke, L.E.; Norcia, M.; Desbonnet, C.R.; Wang, H.; Freeman-Cook, K.; Dougherty, T.J. Identification of an inhibitor of the MurC enzyme, which catalyzes an essential step in the peptidoglycan precursor synthesis pathway. Assay Drug Dev. Technol., 2008, 6(1), 95-103.
[http://dx.doi.org/10.1089/adt.2007.114] [PMID: 18315498]
[47]
Frlan, R.; Kovač, A.; Blanot, D.; Gobec, S.; Pečar, S.; Obreza, A. Design, synthesis and in-vitro biochemical activity of novel amino acid sulfonohydrazide inhibitors of MurC. Acta Chim. Slov., 2011, 58(2), 295-310.
[PMID: 24062040]
[48]
Šink, R.; Kovač, A.; Tomasić, T.; Rupnik, V.; Boniface, A.; Bostock, J.; Chopra, I.; Blanot, D.; Mašic, L.P.; Gobec, S.; Zega, A. Synthesis and biological evaluation of N-acylhydrazones as inhibitors of MurC and MurD ligases. Chem. Med. Chem., 2008, 3(9), 1362-1370.
[http://dx.doi.org/10.1002/cmdc.200800087] [PMID: 18651694]
[49]
Rausch, S.; Hänchen, A.; Denisiuk, A.; Löhken, M.; Schneider, T.; Süssmuth, R.D. Feglymycin is an inhibitor of the enzymes MurA and MurC of the peptidoglycan biosynthesis pathway. Chem. Bio. Chem., 2011, 12(8), 1171-1173.
[http://dx.doi.org/10.1002/cbic.201100120] [PMID: 21538763]
[50]
Vértesy, L.; Aretz, W.; Knauf, M.; Markus, A.; Vogel, M.; Wink, J. Feglymycin, a novel inhibitor of the replication of the human immunodeficiency virus. Fermentation, isolation and structure elucidation. J. Antibiot. (Tokyo), 1999, 52(4), 374-382.
[http://dx.doi.org/10.7164/antibiotics.52.374] [PMID: 10395273]
[51]
Férir, G.; Hänchen, A.; François, K.O.; Hoorelbeke, B.; Huskens, D.; Dettner, F.; Süssmuth, R.D.; Schols, D. Feglymycin, a unique natural bacterial antibiotic peptide, inhibits HIV entry by targeting the viral envelope protein gp120. Virology, 2012, 433(2), 308-319.
[http://dx.doi.org/10.1016/j.virol.2012.08.007] [PMID: 22959895]
[52]
Dettner, F.; Hänchen, A.; Schols, D.; Toti, L.; Nusser, A.; Süssmuth, R.D. Total synthesis of the antiviral peptide antibiotic feglymycin. Angew. Chem. Int. Ed. Engl., 2009, 48(10), 1856-1861.
[http://dx.doi.org/10.1002/anie.200804130] [PMID: 19180618]
[53]
Fuse, S.; Mifune, Y.; Nakamura, H.; Tanaka, H. Total synthesis of feglymycin based on a linear/convergent hybrid approach using micro-flow amide bond formation. Nat. Commun., 2016, 7, 13491-13497.
[http://dx.doi.org/10.1038/ncomms13491] [PMID: 27892469]
[54]
Hänchen, A.; Rausch, S.; Landmann, B.; Toti, L.; Nusser, A.; Süssmuth, R.D. Alanine scan of the peptide antibiotic feglymycin: assessment of amino acid side chains contributing to antimicrobial activity. Chem. Bio. Chem., 2013, 14(5), 625-632.
[http://dx.doi.org/10.1002/cbic.201300032] [PMID: 23447362]
[55]
Šink, R.; Barreteau, H.; Patin, D.; Mengin-Lecreulx, D.; Gobec, S.; Blanot, D. MurD enzymes: some recent developments. Biomol. Concepts, 2013, 4(6), 539-556.
[http://dx.doi.org/10.1515/bmc-2013-0024] [PMID: 25436755]
[56]
Bratkovič, T.; Lunder, M.; Urleb, U.; Štrukelj, B. Peptide inhibitors of MurD and MurE, essential enzymes of bacterial cell wall biosynthesis. J. Basic Microbiol., 2008, 48(3), 202-206.
[http://dx.doi.org/10.1002/jobm.200700133] [PMID: 18506905]
[57]
Paradis-Bleau, C.; Beaumont, M.; Boudreault, L.; Lloyd, A.; Sanschagrin, F.; Bugg, T.D.H.; Levesque, R.C. Selection of peptide inhibitors against the Pseudomonas aeruginosa MurD cell wall enzyme. Peptides, 2006, 27(7), 1693-1700.
[http://dx.doi.org/10.1016/j.peptides.2006.01.017] [PMID: 16517013]
[58]
Horton, J.R.; Bostock, J.M.; Chopra, I.; Hesse, L.; Phillips, S.E.V.; Adams, D.J.; Johnson, A.P.; Fishwick, C.W. Macrocyclic inhibitors of the bacterial cell wall biosynthesis enzyme MurD. Bioorg. Med. Chem. Lett., 2003, 13(9), 1557-1560.
[http://dx.doi.org/10.1016/S0960-894X(03)00176-8] [PMID: 12699754]
[59]
Li, Z.; Francisco, G.D.; Hu, W.; Labthavikul, P.; Petersen, P.J.; Severin, A.; Singh, G.; Yang, Y.; Rasmussen, B.A.; Lin, Y-I.; Skotnicki, J.S.; Mansour, T.S. 2-Phenyl-5,6-dihydro-2H-thieno[3,2-c]pyrazol-3-ol derivatives as new inhibitors of bacterial cell wall biosynthesis. Bioorg. Med. Chem. Lett., 2003, 13(15), 2591-2594.
[http://dx.doi.org/10.1016/S0960-894X(03)00471-2] [PMID: 12852973]
[60]
Antane, S.; Caufield, C.E.; Hu, W.; Keeney, D.; Labthavikul, P.; Morris, K.; Naughton, S.M.; Petersen, P.J.; Rasmussen, B.A.; Singh, G.; Yang, Y. Pulvinones as bacterial cell wall biosynthesis inhibitors. Bioorg. Med. Chem. Lett., 2006, 16(1), 176-180.
[http://dx.doi.org/10.1016/j.bmcl.2005.09.021] [PMID: 16216496]
[61]
Turk, S.; Kovač, A.; Boniface, A.; Bostock, J.M.; Chopra, I.; Blanot, D.; Gobec, S. Discovery of new inhibitors of the bacterial peptidoglycan biosynthesis enzymes MurD and MurF by structure-based virtual screening. Bioorg. Med. Chem., 2009, 17(5), 1884-1889.
[http://dx.doi.org/10.1016/j.bmc.2009.01.052] [PMID: 19223185]
[62]
Frlan, R.; Kovač, A.; Blanot, D.; Gobec, S.; Pečar, S.; Obreza, A. Design and synthesis of novel N-benzylidenesulfonohydrazide inhibitors of MurC and MurD as potential antibacterial agents. Molecules, 2008, 13(1), 11-30.
[http://dx.doi.org/10.3390/molecules13010011] [PMID: 18259126]
[63]
Tomasić, T.; Zidar, N.; Kovač, A.; Turk, S.; Simčič, M.; Blanot, D.; Müller-Premru, M.; Filipič, M.; Grdadolnik, S.G.; Zega, A.; Anderluh, M.; Gobec, S.; Kikelj, D.; Peterlin Mašič, L. 5-Benzylidenethiazolidin-4-ones as multitarget inhibitors of bacterial Mur ligases. Chem. Med. Chem., 2010, 5(2), 286-295.
[http://dx.doi.org/10.1002/cmdc.200900449] [PMID: 20024979]
[64]
Perdih, A.; Kovač, A.; Wolber, G.; Blanot, D.; Gobec, S.; Solmajer, T. Discovery of novel benzene 1,3-dicarboxylic acid inhibitors of bacterial MurD and MurE ligases by structure-based virtual screening approach. Bioorg. Med. Chem. Lett., 2009, 19(10), 2668-2673.
[http://dx.doi.org/10.1016/j.bmcl.2009.03.141] [PMID: 19369074]
[65]
Tanner, M.E.; Vaganay, S.; van Heijenoort, J.; Blanot, D. Phosphinate inhibitors of the D-glutamic acid-adding enzyme of peptidoglycan biosynthesis. J. Org. Chem., 1996, 61(5), 1756-1760.
[http://dx.doi.org/10.1021/jo951780a] [PMID: 11667046]
[66]
Zeng, B.; Wong, K.K.; Pompliano, D.L.; Reddy, S.; Tanner, M.E. A phosphinate inhibitor of the meso-diaminopimelic acid-adding enzyme (MurE) of peptidoglycan biosynthesis. J. Org. Chem., 1998, 63, 10081-10086.
[http://dx.doi.org/10.1021/jo981895p]
[67]
Gegnas, L.D.; Waddell, S.T.; Chabin, R.M.; Reddy, S.; Wong, K.K. Inhibitors of the bacterial cell wall biosynthesis enzyme MurD. Bioorg. Med. Chem. Lett., 1998, 8(13), 1643-1648.
[http://dx.doi.org/10.1016/S0960-894X(98)00285-6] [PMID: 9873406]
[68]
Štrancar, K.; Blanot, D.; Gobec, S. Design, synthesis and structure-activity relationships of new phosphinate inhibitors of MurD. Bioorg. Med. Chem. Lett., 2006, 16(2), 343-348.
[http://dx.doi.org/10.1016/j.bmcl.2005.09.086] [PMID: 16271472]
[69]
Zidar, N.; Tomasić, T.; Šink, R.; Rupnik, V.; Kovač, A.; Turk, S.; Patin, D.; Blanot, D.; Contreras Martel, C.; Dessen, A.; Müller Premru, M.; Zega, A.; Gobec, S.; Peterlin Mašič, L.; Kikelj, D. Discovery of novel 5-benzylidenerhodanine and 5-benzylidenethiazolidine-2,4-dione inhibitors of MurD ligase. J. Med. Chem., 2010, 53(18), 6584-6594.
[http://dx.doi.org/10.1021/jm100285g] [PMID: 20804196]
[70]
Tomašić, T.; Kovač, A.; Simčič, M.; Blanot, D.; Grdadolnik, S.G.; Gobec, S.; Kikelj, D.; Peterlin Mašič, L. Novel 2-thioxothiazolidin-4-one inhibitors of bacterial MurD ligase targeting D-Glu- and diphosphate-binding sites. Eur. J. Med. Chem., 2011, 46(9), 3964-3975.
[http://dx.doi.org/10.1016/j.ejmech.2011.05.070] [PMID: 21703731]
[71]
Tomašić, T.; Šink, R.; Zidar, N.; Fic, A.; Contreras-Martel, C.; Dessen, A.; Patin, D.; Blanot, D.; Müller-Premru, M.; Gobec, S.; Zega, A.; Kikelj, D.; Mašič, L.P. Dual inhibitor of MurD and MurE ligases from Escherichia coli and Staphylococcus aureus. ACS Med. Chem. Lett., 2012, 3(8), 626-630.
[http://dx.doi.org/10.1021/ml300047h] [PMID: 24900523]
[72]
Humljan, J.; Kotnik, M.; Contreras-Martel, C.; Blanot, D.; Urleb, U.; Dessen, A.; Šolmajer, T.; Gobec, S. Novel naphthalene-N-sulfonyl-D-glutamic acid derivatives as inhibitors of MurD, a key peptidoglycan biosynthesis enzyme. J. Med. Chem., 2008, 51(23), 7486-7494.
[http://dx.doi.org/10.1021/jm800762u] [PMID: 19007109]
[73]
Kotnik, M.; Humljan, J.; Contreras-Martel, C.; Oblak, M.; Kristan, K.; Hervé, M.; Blanot, D.; Urleb, U.; Gobec, S.; Dessen, A.; Solmajer, T. Structural and functional characterization of enantiomeric glutamic acid derivatives as potential transition state analogue inhibitors of MurD ligase. J. Mol. Biol., 2007, 370(1), 107-115.
[http://dx.doi.org/10.1016/j.jmb.2007.04.048] [PMID: 17507028]
[74]
Sosič, I.; Barreteau, H.; Simčič, M.; Šink, R.; Cesar, J.; Zega, A.; Grdadolnik, S.G.; Contreras-Martel, C.; Dessen, A.; Amoroso, A.; Joris, B.; Blanot, D.; Gobec, S. Second-generation sulfonamide inhibitors of D-glutamic acid-adding enzyme: activity optimisation with conformationally rigid analogues of D-glutamic acid. Eur. J. Med. Chem., 2011, 46(7), 2880-2894.
[http://dx.doi.org/10.1016/j.ejmech.2011.04.011] [PMID: 21524830]
[75]
Samal, H.B.; Das, J.K.; Mahapatra, R.K.; Suar, M. Molecular modeling, simulation and virtual screening of MurD ligase protein from Salmonella typhimurium LT2. J. Pharmacol. Toxicol. Methods, 2015, 73, 34-41.
[http://dx.doi.org/10.1016/j.vascn.2015.03.005] [PMID: 25841669]
[76]
Bouhss, A.; Mengin-Lecreulx, D.; Blanot, D.; van Heijenoort, J.; Parquet, C. Invariant amino acids in the Mur peptide synthetases of bacterial peptidoglycan synthesis and their modification by site-directed mutagenesis in the UDP-MurNAc:L-alanine ligase from Escherichia coli. Biochemistry, 1997, 36(39), 11556-11563.
[http://dx.doi.org/10.1021/bi970797f] [PMID: 9305945]
[77]
Schleifer, K.H.; Kandler, O. Peptidoglycan types of bacterial cell walls and their taxonomic implications. Bacteriol. Rev., 1972, 36(4), 407-477.
[http://dx.doi.org/10.1128/MMBR.36.4.407-477.1972] [PMID: 4568761]
[78]
Guzman, J.D.; Gupta, A.; Evangelopoulos, D.; Basavannacharya, C.; Pabon, L.C.; Plazas, E.A.; Muñoz, D.R.; Delgado, W.A.; Cuca, L.E.; Ribon, W.; Gibbons, S.; Bhakta, S. Anti-tubercular screening of natural products from Colombian plants: 3-methoxynordomesticine, an inhibitor of MurE ligase of Mycobacterium tuberculosis. J. Antimicrob. Chemother., 2010, 65(10), 2101-2107.
[http://dx.doi.org/10.1093/jac/dkq313] [PMID: 20719764]
[79]
Mata, R.; Morales, I.; Pérez, O.; Rivero-Cruz, I.; Acevedo, L.; Enriquez-Mendoza, I.; Bye, R.; Franzblau, S.; Timmermann, B. Antimycobacterial compounds from Piper sanctum. J. Nat. Prod., 2004, 67(12), 1961-1968.
[http://dx.doi.org/10.1021/np0401260] [PMID: 15620234]
[80]
Shiu, W.K.P.; Malkinson, J.P.; Rahman, M.M.; Curry, J.; Stapleton, P.; Gunaratnam, M.; Neidle, S.; Mushtaq, S.; Warner, M.; Livermore, D.M.; Evangelopoulos, D.; Basavannacharya, C.; Bhakta, S.; Schindler, B.D.; Seo, S.M.; Coleman, D.; Kaatz, G.W.; Gibbons, S. A new plant-derived antibacterial is an inhibitor of efflux pumps in Staphylococcus aureus. Int. J. Antimicrob. Agents, 2013, 42(6), 513-518.
[http://dx.doi.org/10.1016/j.ijantimicag.2013.08.007] [PMID: 24119569]
[81]
Guzman, J.D.; Wube, A.; Evangelopoulos, D.; Gupta, A.; Hüfner, A.; Basavannacharya, C.; Rahman, M.M.; Thomaschitz, C.; Bauer, R.; McHugh, T.D.; Nobeli, I.; Prieto, J.M.; Gibbons, S.; Bucar, F.; Bhakta, S. Interaction of N-methyl-2-alkenyl-4-quinolones with ATP-dependent MurE ligase of Mycobacterium tuberculosis: antibacterial activity, molecular docking and inhibition kinetics. J. Antimicrob. Chemother., 2011, 66(8), 1766-1772.
[http://dx.doi.org/10.1093/jac/dkr203] [PMID: 21622974]
[82]
Miller, D.J.; Hammond, S.M.; Anderluzzi, D.; Bugg, T.D.H. Aminoalkylphosphinate inhibitors of D-Ala-D-Ala adding enzyme. J. Chem. Soc., Perkin Trans., 1998, 1, 131-142.
[http://dx.doi.org/10.1039/a704097k]
[83]
Comess, K.M.; Schurdak, M.E.; Voorbach, M.J.; Coen, M.; Trumbull, J.D.; Yang, H.; Gao, L.; Tang, H.; Cheng, X.; Lerner, C.G.; McCall, J.O.; Burns, D.J.; Beutel, B.A. An ultraefficient affinity-based high-throughout screening process: application to bacterial cell wall biosynthesis enzyme MurF. J. Biomol. Screen., 2006, 11(7), 743-754.
[http://dx.doi.org/10.1177/1087057106289971] [PMID: 16973923]
[84]
Longenecker, K.L.; Stamper, G.F.; Hajduk, P.J.; Fry, E.H.; Jakob, C.G.; Harlan, J.E.; Edalji, R.; Bartley, D.M.; Walter, K.A.; Solomon, L.R.; Holzman, T.F.; Gu, Y.G.; Lerner, C.G.; Beutel, B.A.; Stoll, V.S. Structure of MurF from Streptococcus pneumoniae co-crystallized with a small molecule inhibitor exhibits interdomain closure. Protein Sci., 2005, 14(12), 3039-3047.
[http://dx.doi.org/10.1110/ps.051604805] [PMID: 16322581]
[85]
Gu, Y.G.; Florjancic, A.S.; Clark, R.F.; Zhang, T.; Cooper, C.S.; Anderson, D.D.; Lerner, C.G.; McCall, J.O.; Cai, Y.; Black-Schaefer, C.L.; Stamper, G.F.; Hajduk, P.J.; Beutel, B.A. Structure-activity relationships of novel potent MurF inhibitors. Bioorg. Med. Chem. Lett., 2004, 14(1), 267-270.
[http://dx.doi.org/10.1016/j.bmcl.2003.09.073] [PMID: 14684340]
[86]
Stamper, G.F.; Longenecker, K.L.; Fry, E.H.; Jakob, C.G.; Florjancic, A.S.; Gu, Y-G.; Anderson, D.D.; Cooper, C.S.; Zhang, T.; Clark, R.F.; Cia, Y.; Black-Schaefer, C.L.; Owen McCall, J.; Lerner, C.G.; Hajduk, P.J.; Beutel, B.A.; Stoll, V.S. Structure-based optimization of MurF inhibitors. Chem. Biol. Drug Des., 2006, 67(1), 58-65.
[http://dx.doi.org/10.1111/j.1747-0285.2005.00317.x] [PMID: 16492149]
[87]
Hrast, M.; Turk, S.; Sosič, I.; Knez, D.; Randall, C.P.; Barreteau, H.; Contreras-Martel, C.; Dessen, A.; O’Neill, A.J.; Mengin-Lecreulx, D.; Blanot, D.; Gobec, S. Structure-activity relationships of new cyanothiophene inhibitors of the essential peptidoglycan biosynthesis enzyme MurF. Eur. J. Med. Chem., 2013, 66, 32-45.
[http://dx.doi.org/10.1016/j.ejmech.2013.05.013] [PMID: 23786712]
[88]
Hrast, M.; Anderluh, M.; Knez, D.; Randall, C.P.; Barreteau, H.; O’Neill, A.J.; Blanot, D.; Gobec, S. Design, synthesis and evaluation of second generation MurF inhibitors based on a cyanothiophene scaffold. Eur. J. Med. Chem., 2014, 73, 83-96.
[http://dx.doi.org/10.1016/j.ejmech.2013.11.031] [PMID: 24384549]
[89]
Baum, E.Z.; Crespo-Carbone, S.M.; Klinger, A.; Foleno, B.D.; Turchi, I.; Macielag, M.; Bush, K. A MurF inhibitor that disrupts cell wall biosynthesis in Escherichia coli. Antimicrob. Agents Chemother., 2007, 51(12), 4420-4426.
[http://dx.doi.org/10.1128/AAC.00845-07] [PMID: 17908943]
[90]
Baum, E.Z.; Crespo-Carbone, S.M.; Foleno, B.D.; Simon, L.D.; Guillemont, J.; Macielag, M.; Bush, K.; Mur, F. MurF inhibitors with antibacterial activity: effect on muropeptide levels. Antimicrob. Agents Chemother., 2009, 53(8), 3240-3247.
[http://dx.doi.org/10.1128/AAC.00166-09] [PMID: 19470511]
[91]
Sosič, I.; Štefane, B.; Kovač, A.; Turk, S.; Blanot, D.; Gobec, S. The synthesis of novel 2,4,6-trisubstituted 1,3,5-triazines: a search for potential MurF enzyme inhibitors. Heterocycles, 2010, 81, 91-115.
[http://dx.doi.org/10.3987/COM-09-11839]
[92]
Turk, S.; Hrast, M.; Sosič, I.; Barreteau, H.; Mengin-Lecreulx, D.; Blanot, D.; Gobec, S. Biochemical characterization of MurF from Streptococcus pneumoniae and the identification of a new MurF inhibitor through ligand-based virtual screening. Acta Chim. Slov., 2013, 60(2), 294-299.
[PMID: 23878932]
[93]
Sova, M.; Kovač, A.; Turk, S.; Hrast, M.; Blanot, D.; Gobec, S. Phosphorylated hydroxyethylamines as novel inhibitors of the bacterial cell wall biosynthesis enzymes MurC to MurF. Bioorg. Chem., 2009, 37(6), 217-222.
[http://dx.doi.org/10.1016/j.bioorg.2009.09.001] [PMID: 19804894]
[94]
Bauer, R.; Dicks, L.M.T. Mode of action of lipid II-targeting lantibiotics. Int. J. Food Microbiol., 2005, 101(2), 201-216.
[http://dx.doi.org/10.1016/j.ijfoodmicro.2004.11.007] [PMID: 15862882]
[95]
Ling, L.L.; Schneider, T.; Peoples, A.J.; Spoering, A.L.; Engels, I.; Conlon, B.P.; Mueller, A.; Schäberle, T.F.; Hughes, D.E.; Epstein, S.; Jones, M.; Lazarides, L.; Steadman, V.A.; Cohen, D.R.; Felix, C.R.; Fetterman, K.A.; Millett, W.P.; Nitti, A.G.; Zullo, A.M.; Chen, C.; Lewis, K. A new antibiotic kills pathogens without detectable resistance. Nature, 2015, 517(7535), 455-459.
[http://dx.doi.org/10.1038/nature14098] [PMID: 25561178]
[96]
Liu, Y.; Liu, Y.; Chan-Park, M.B.; Mu, Y. Binding modes of teixobactin to lipid II: molecular dynamics study. Sci. Rep., 2017, 7(1), 17197-17208.
[http://dx.doi.org/10.1038/s41598-017-17606-5] [PMID: 29222455]

Rights & Permissions Print Cite
Article Metrics
52
7
© 2024 Bentham Science Publishers | Privacy Policy