Discovery of environment-sensitive fluorescent probes for detecting and inhibiting metallo-β-lactamase

Chen, 2022, Structure and mechanism-guided design of dual serine/metallo- carbapenemase inhibitors, J. Med. Chem., 65, 5954, 10.1021/acs.jmedchem.2c00213 Boyce, 2020, Platform to discover protease-activated antibiotics and application to siderophore-antibiotic conjugates, J. Am. Chem. Soc., 142, 21310, 10.1021/jacs.0c06987 Yan, 2020, Principles and current strategies targeting metallo-β-lactamase mediated antibacterial resistance, Med. Res. Rev., 40, 1558, 10.1002/med.21665 Bush, 2019, Interplay between β-lactamases and new β-lactamase inhibitors, Nat. Rev. Microbiol., 17, 295, 10.1038/s41579-019-0159-8 González-Bello, 2020, β-lactamase inhibitors to restore the efficacy of antibiotics against superbugs, J. Med. Chem., 63, 1859, 10.1021/acs.jmedchem.9b01279 King, 2014, AMA overcomes metallo-β-lactamase antibiotic resistance, Nature, 510, 503, 10.1038/nature13445 Palacios, 2020, Metallo-β-lactamase inhibitors inspired on snapshots from the catalytic mechanism, Biomolecules, 10, 854, 10.3390/biom10060854 Chen, 2020, Structure-based design of covalent inhibitors targeting metallo-β-lactamases, Eur. J. Med. Chem., 203, 10.1016/j.ejmech.2020.112573 Sun, 2020, Resensitizing carbapenem- and colistin-resistant bacteria to antibiotics using auranofin, Nat. Commun., 11, 5263, 10.1038/s41467-020-18939-y Krajnc, 2019, Bicyclic boronate VNRX-5133 inhibits metallo- and serine-β-lactamases, J. Med. Chem., 62, 8544, 10.1021/acs.jmedchem.9b00911 C. López, J. Delmonti, R.A. Bonomo, A.J. Vila, Deciphering the evolution of metallo-β-lactamases: A journey from the test tube to the bacterial periplasm, J. Biol. Chem. 298 (2022) 101665. Ding, 2021, Fluorogenic probes/inhibitors of β-lactamase and their applications in drug-resistant bacteria, Angew. Chem. Int. Ed., 60, 24, 10.1002/anie.202006635 Mehta, 2021, Visualizing the dynamic metalation state of New Delhi Metallo-β-lactamase-1 in bacteria using a reversible fluorescent probe, J. Am. Chem. Soc., 143, 8314, 10.1021/jacs.1c00290 Song, 2017, Intramolecular substitution uncages fluorogenic probes for detection of metallo-carbapenemase-expressing bacteria, Chem. Sci., 8, 7669, 10.1039/C7SC02416A Xie, 2021, A dual-caged resorufin probe for rapid screening of infections resistant to lactam antibiotics, Chem. Sci., 12, 9153, 10.1039/D1SC01471D Cheng, 2018, Rapid and specific labeling of single live Mycobacterium tuberculosis with a dual-targeting fluorogenic probe, Sci. Transl. Med., 10, eaar4470, 10.1126/scitranslmed.aar4470 Xie, 2012, Rapid point-of-care detection of the tuberculosis pathogen using a BlaC-specific fluorogenic probe, Nat. Chem., 4, 802, 10.1038/nchem.1435 Mao, 2017, Detection of carbapenemase-producing organisms with a carbapenem-based fluorogenic probe, Angew. Chem. Int. Ed., 56, 4468, 10.1002/anie.201612495 Mao, 2019, A carbapenem-based off-on fluorescent probe for specific detection of metallo-β-lactamase activities, Chembiochem., 20, 511, 10.1002/cbic.201800126 Ma, 2021, Rapid broad spectrum detection of carbapenemases with a dual fluorogenic-colorimetric probe, J. Am. Chem. Soc., 143, 6886, 10.1021/jacs.1c00462 Mehta, 2021, Visualizing the dynamic metalation state of New Delhi Metallo-βlactamase-1 in bacteria using a reversible fluorescent probe, J. Am. Chem. Soc., 143, 8314, 10.1021/jacs.1c00290 Chiou, 2015, Ebselen as a potent covalent inhibitor of New Delhi metallo-β-lactamase (NDM-1), Chem. Commun., 51, 9543, 10.1039/C5CC02594J Chen, 2019, The assemblage of covalent and metal binding dual functional scaffold for cross-class metallo-β-lactamases inhibition, Future Med. Chem., 11, 2381, 10.4155/fmc-2019-0008 Liu, 2020, meta-Substituted benzenesulfonamide: a potent scaffold for the development of metallo-β-lactamase ImiS inhibitors, RSC Med. Chem., 11, 259, 10.1039/C9MD00455F Chang, 2017, Carbamylmethyl mercaptoacetate thioether: a novel scaffold for the development of L1 metallo-β-lactamase inhibitors, ACS Med. Chem. Let., 8, 527, 10.1021/acsmedchemlett.7b00058 Zhang, 2018, Real-time monitoring of NDM-1 activity in live bacterial cells by isothermal titration calorimetry: a new approach to measure inhibition of antibiotic-resistant bacteria, ACS Infect. Dis., 4, 1671, 10.1021/acsinfecdis.8b00147 Chen, 2018, Mercaptoacetate thioesters and their hydrolysate mercaptoacetic acids jointly inhibit metallo-β-lactamase L1, Med. Chem. Commun., 9, 1172, 10.1039/C8MD00091C Wang, 2019, Structure-based development of (1-(3'-Mercaptopropanamido)methyl)boronic acid derived broad-spectrum, dual-action inhibitors of metallo- and serine-β-lactamases, J. Med. Chem., 62, 7160, 10.1021/acs.jmedchem.9b00735 Xiang, 2018, Rhodanine as a potent scaffold for the development of broad-spectrum metallo-β-lactamase inhibitors, ACS Med. Chem. Let., 9, 359, 10.1021/acsmedchemlett.7b00548 Liu, 2016, Environment-sensitive fluorescent probe for the human ether-a-go-go-related gene potassium channel, Anal. Chem., 88, 1511, 10.1021/acs.analchem.5b04220 Liu, 2017, Discovery of a turn-on fluorescent probe for myeloid cell leukemia-1 protein, Anal. Chem., 89, 11173, 10.1021/acs.analchem.7b01148 Liu, 2019, Discovery of Turn-On Fluorescent Probes for Detecting Bcl-2 Protein, Anal. Chem., 91, 5722, 10.1021/acs.analchem.8b05853 Wu, 2021, A theranostic probe of indoleamine 2,3-dioxygenase 1 (IDO1) for small molecule cancer immunotherapy, Eur. J. Med. Chem., 213, 10.1016/j.ejmech.2021.113163 Chen, 2018, A protein structure-guided covalent scaffold selectively targets the B1 and B2 subclass metallo-β-lactamases, Chem. Commun., 54, 4802, 10.1039/C8CC01067F Bianco, 2016, Covalent docking using autodock: Two-point attractor and flexible side chain methods, Protein Sci., 25, 295, 10.1002/pro.2733 Chen, 2020, Disulfiram as a potent metallo-β-lactamase inhibitor with dual functional mechanisms, Chem. Commun., 56, 2755, 10.1039/C9CC09074F Lomovskaya, 2020, Biochemical characterization of QPX7728, a new ultrabroad-spectrum beta-lactamase inhibitor of serine and metallo-β-lactamases, Antimicrob. Agents Chemother., 64, e00130, 10.1128/AAC.00552-20 Chen, 2020, Ruthenium complexes as prospective inhibitors of metallo-β-lactamases to reverse carbapenem resistance, Dalton Trans., 49, 14099, 10.1039/D0DT02430A Chen, 2019, Ebselen bearing polar functionality: Identification of potent antibacterial agents against multidrug-resistant Gram-negative bacteria, Bioorg. Chem., 93, 10.1016/j.bioorg.2019.103286 Macegoniuk, 2016, 1,2-Benzisoselenazol-3(2H)-one derivatives as a new class of bacterial urease inhibitors, J. Med. Chem., 59, 8125, 10.1021/acs.jmedchem.6b00986