Design, synthesis and biological evaluation of non-covalent AmpC β-lactamases inhibitors

Medicinal Chemistry Research

Volumn 26, Issue 5, 2017, Pages 975-986

  Genovese, Filippo ^a   Lazzari, Sandra ^a   Venturi, Ettore ^a   Costantino, Luca ^a   Blazquez, Jesus ^b,c   Ibacache Quiroga, Claudia ^b,c   Costi, Maria Paola ^a   Tondi, Donatella ^a  

^a UNIVERSITY OF MODENA AND REGGIO EMILIA   (Italy)

^b Instituto de Biomedicina de Sevilla   (Spain)

^c CENTRO NACIONAL DE BIOTECNOLOGÍA   (Spain)

Author keywords

Minimum inhibitory concentration (MIC); Non covalent lactamases inhibitor; Structure based de novo design; Synthesis; Thiophene derivatives

Indexed keywords

2 (3 NITROPHENYL)PROPIONITRILE; 2 AMINO [3 [2 (METHOXYCARBONYL)THIOPHEN 3 SULFONAMIDO]PHENYL]ACETIC ACID; 3 [(1 CARBOXYETHYL)SULFAMOYL]THIOPHENE 2 CARBOXYLIC ACID; 3 [(2 CARBOXYETHYL)SULFAMOYL]THIOPHENE 2 CARBOXYLIC ACID; 3 [(CARBOXYMETHYL)SULFAMOYL]THIOPHENE 2 CARBOXYLIC ACID; 3 [3 [[[2 (METHOXYCARBONYL)THIOPHEN 3 YL]SULFONYL]AMINO]PHENYL]PROPANOIC ACID; 3 [[3 (1 CARBOXYETHYL)PHENYL]SULFAMOYL]THIOPHENE 2 CARBOXYLIC ACID; 3 [[3 (2 CARBOXYETHYL)PHENYL]SULFAMOYL]THIOPHENE 2 CARBOXYLIC ACID; 3 [[3 (2H TETRAZOL 5 YLMETHYL)PHENYL]SULFAMOYL]THIOPHENE 2 CARBOXYLIC ACID; 3 [[3 (CARBOXYMETHYL) 2,4 DIFLUOROPHENYL]SULFAMOYL]THIOPHENE 2 CARBOXYLIC ACID; 3 [[3 (CARBOXYMETHYL)PHENYL]SULFAMOYL]THIOPHENE 2 CARBOXYLIC ACID; 3 [[3 [CARBOXY(CARBOXYAMINO)METHYL]PHENYL]SULFAMOYL]THIOPHENE 2 CARBOXYLIC ACID; 3 [[4 (CARBOXYMETHYL)PHENYL]SULFAMOYL]THIOPHENE 2 CARBOXYLIC ACID; AMINO (3 NITROPHENYL)ACETIC ACID; ANTIBIOTIC AGENT; BETA LACTAMASE AMPC; CEPHALOSPORIN; ETHYL 2 (3 AMINOPHENYL)PROPIONATE; ETHYL 2 (3 NITROPHENYL)PROPIONATE; HYDROLASE INHIBITOR; METHYL 3 [(1 METHOXY 1 OXOPROPAN 2 YL)SULFAMOYL]THIOPHENE 2 CARBOXYLATE; METHYL 3 [(2 ETHOXY 2 OXOETHYL)SULFAMOYL]THIOPHENE 2 CARBOXYLATE; METHYL 3 [(3 ETHOXY 3 OXOPROPYL)SULFAMOYL]THIOPHENE 2 CARBOXYLATE; METHYL 3 [[2,4 DIFLUORO 3 (2 METHOXY 2 OXOETHYL)PHENYL]SULFAMOYL]THIOPHENE 2 CARBOXYLATE; METHYL 3 [[3 (1 ETHOXY 1 OXOPROPAN 2 YL)PHENYL]SULFAMOYL]THIOPHENE 2 CARBOXYLATE; METHYL 3 [[3 (1 [[(TERT BUTOXY)CARBONYL]AMINO] 2 METHOXY 2 OXOETHYL]PHENYL]SULFAMOYL]THIOPHENE 2 CARBOXYLATE; THIOPHENE DERIVATIVE; UNCLASSIFIED DRUG; UNINDEXED DRUG; [3 [[[2 (METHOXYCARBONYL)THIOPHEN 3 YL]SULFONYL]AMINO]PHENYL]ACETIC ACID; [4 [[[2 (METHOXYCARBONYL)THIOPHEN 3 YL]SULFONYL]AMINO]PHENYL]ACETIC ACID;

ANTIBACTERIAL ACTIVITY; ANTIBIOTIC RESISTANCE; ARTICLE; BACTERIAL STRAIN; BACTERIUM CULTURE; BACTERIUM ISOLATION; CARBON NUCLEAR MAGNETIC RESONANCE; CONTROLLED STUDY; DRUG BINDING SITE; DRUG DESIGN; DRUG POTENCY; DRUG POTENTIATION; DRUG STRUCTURE; DRUG SYNTHESIS; ENTEROBACTER AEROGENES; ENTEROBACTER CLOACAE; ESCHERICHIA COLI; HYDROGEN BOND; IC50; IN VITRO STUDY; KLEBSIELLA PNEUMONIAE; MASS SPECTROMETRY; MINIMUM INHIBITORY CONCENTRATION; NONHUMAN; PROTON NUCLEAR MAGNETIC RESONANCE; PSEUDOMONAS AERUGINOSA; THIN LAYER CHROMATOGRAPHY; ULTRAVIOLET RADIATION;

EID: 85014074574     PISSN: 10542523     EISSN: 15548120     Source Type: Journal    
DOI: 10.1007/s00044-017-1809-x     Document Type: Article

References (26)

1. Babaoglu K, Shoichet BK (2006) Deconstructing fragment-based inhibitor discovery. Nat Chem Biol 2:720–723
2. Ballatore C, Huryn DM, Smith AB (2013) Carboxylic acid (bio)isosteres in drug design. Chem Med Chem 8:385–395
3. Bush K, Jacoby A (2010) Updated functional classification of β-lactamases. Antimicrob Agents Chemother 54:969–976
4. Clinical and Laboratory Standards Institute (2010) Performance standards for antimicrobial susceptibility testing. 20th Informational Supplement M100–S209. http://clsi.org/blog/2015/01/08/clsi-publishes-new-antimicrobial-susceptibility-testing-standards/
5. Cosgrove S, Carmeli Y (2003) The impact of antimicrobial resistance on health and economic outcomes. Clin Infect Dis 36:1433–1437
6. Drawz SM, Bonomo RA (2010) Three decades of β-lactamase inhibitors. Clin Microbiol Rev 23:160–201
7. Eidam O, Romagnoli C, Caselli E, Babaoglu K, Pohlhaus DT, Karpiak J, Bonnet R, Shoichet BK, Prati F (2010) Design, synthesis, crystal structures, and antimicrobial activity of sulfonamide boronic acids as beta-lactamase inhibitors. J Med Chem 53:7852–7863
8. Eidam O, Romagnoli C, Dalmasso G, Barelier S, Caselli E, Bonnet R, Shoichet BK, Prati F (2012) Fragment-guided design of subnanomolar beta-lactamase inhibitors active in vivo. Proc Natl Acad Sci USA 109:17448–17453
9. Farina D, Spyrakis F, Venturelli A, Cross S, Tondi D, Costi MP (2014) The inhibition of extended spectrum β-lactamases: hits and leads. Curr Med Chem 21:1405–1434
10. Hecker SJ, Reddy KR, Totrov M, Hirst GC, Lomovskaya O, Griffith DC, King P, Tsivkovski R, Sun D1, Sabet M, Tarazi Z, Clifton MC, Atkins K, Raymond A, Potts KT, Abendroth J, Boyer SH, Loutit JS, Morgan EE, Durso S, Dudley MN (2015) Discovery of a cyclic boronic acid β-lactamase inhibitor (RPX7009) with utility vs class A Serine carbapenemases. J Med Chem 58:3682–3692
11. Hopkins AL, Groom CR, Alex A (2004) Ligand efficiency: a useful metric for lead selection. Drug Discov Today 9:430–431
12. Jacoby GA (2009) AmpC beta-lactamases. Clin Microbiol Rev 22:161–182
13. Kenneth S, Thomson J (2010) Extended-spectrum-β-Lactamase, AmpC, and carbapenemase issues. Clin Microbiol 48:1019–1102
14. Li G, Zhao G (2006) Allylation of aldehydes and imines: promoted by reuseable polymer-supported sulfonamide of N-glycine. Org Lett 8:633–636
15. Nukaga M, Kumar S, Nukaga K, Pratt RF, Knox JR (2004) Hydrolysis of third-generation cephalosporins by class C beta-lactamases: structures of a transition state analog of cefotaxime in wild-type and extended spectrum enzymes. J Biol Chem 279:9344–9352
16. Powers RA, Blazquez J, Weston GS, Morosini MI, Baquero F, Shoichet BK (1999) The complexed structure and antimicrobial activity of a non-beta-lactam inhibitor of AmpC beta-lactamase. Protein Sci 8:2330–2337
17. Powers RA, Morandi F, Shoichet BK (2002) Structure-based discovery of a novel, noncovalent inhibitor of ampc beta-lactamase. Structure 10:1013–1023
18. Rice LB, Bonomo RA (2000) Beta-lactamases: which ones are clinically important? Drug Resist Updates 3:178–189
19. Sassatelli M, Debiton É, Aboab B, Prudhomme M, Moreau P (2006) Synthesis and antiproliferative activities of indolin-2-one derivatives bearing amino acid moieties. Eur J Med Chem 41:709–716
20. Tondi D, Calò S, Shoichet BK, Costi MP (2010) Structural study of phenyl boronic acid derivatives as AmpC β-lactamase inhibitors. Bioorg Med Chem Lett 20(11):3416–3419
21. Tondi D, Cross S, Venturelli A, Costi MP, Cruciani G, Spyrakis F (2016) Decoding the structural basis for carbapenem hydrolysis by class A β- lactamases: fishing for a pharmacophore. Curr Drug Targets 17:983–1005
22. Tondi D, Morandi F, Bonnet R, Costi MP, Shoichet BK (2005) Structure-based optimization of a Non-β-lactam lead results in inhibitors that do not up-regulate β-lactamase expression in cell culture. J Am Chem Soc 127:4632–4639
23. Tondi D, Powers RA, Caselli E, Negri MC, Blázquez J, Costi MP, Shoichet BK (2001) Structure-based design and in-parallel synthesis of inhibitors of AmpC beta-lactamase. Chem Biol 8:593–611
24. Tondi D, Venturelli A, Bonnet R, Pozzi C, Shoichet BK, Costi MP (2014) Targeting class A and C Serine β-lactamases with a broad-spectrum boronic acid derivative. J Med Chem 57:5449–5458
25. Venturelli A, Tondi D, Cancian L, Morandi F, Cannazza G, Segatore B, Prati F, Amicosante G, Shoichet BK, Costi MP (2007) Optimizing cell permeation of an antibiotic resistance inhibitor for improved efficacy. J Med Chem 50:5644–5654
26. World Health Organization (2014) Antimicrobial resistance: global report on surveillance. http://apps.who.int/iris/bitstream/10665/112642/1/9789241564748_eng.pdf. Accessed 23 Feb 2016