@article{belardinelli_li_martin_zeiler_lian_avanzi_wiersma_nguyen_angala_moura_et al._2022, title={2-Aminoimidazoles Inhibit Mycobacterium abscessus Biofilms in a Zinc-Dependent Manner}, volume={23}, ISSN={["1422-0067"]}, DOI={10.3390/ijms23062950}, abstractNote={Biofilm growth is thought to be a significant obstacle to the successful treatment of Mycobacterium abscessus infections. A search for agents capable of inhibiting M. abscessus biofilms led to our interest in 2-aminoimidazoles and related scaffolds, which have proven to display antibiofilm properties against a number of Gram-negative and Gram-positive bacteria, including Mycobacterium tuberculosis and Mycobacterium smegmatis. The screening of a library of 30 compounds led to the identification of a compound, AB-2-29, which inhibits the formation of M. abscessus biofilms with an IC50 (the concentration required to inhibit 50% of biofilm formation) in the range of 12.5 to 25 μM. Interestingly, AB-2-29 appears to chelate zinc, and its antibiofilm activity is potentiated by the addition of zinc to the culture medium. Preliminary mechanistic studies indicate that AB-2-29 acts through a distinct mechanism from those reported to date for 2-aminoimidazole compounds.}, number={6}, journal={INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES}, author={Belardinelli, Juan M. and Li, Wei and Martin, Kevin H. and Zeiler, Michael J. and Lian, Elena and Avanzi, Charlotte and Wiersma, Crystal J. and Nguyen, Tuan Vu and Angala, Bhanupriya and Moura, Vinicius C. N. and et al.}, year={2022}, month={Mar} }
 @article{nguyen_minrovic_melander_melander_2019, title={Identification of Anti-Mycobacterial Biofilm Agents Based on the 2-Aminoimidazole Scaffold}, volume={14}, ISSN={["1860-7187"]}, DOI={10.1002/cmdc.201900033}, abstractNote={AbstractTuberculosis (TB) remains a significant global health problem for which new therapeutic options are sorely needed. The ability of the causative agent, Mycobacterium tuberculosis, to reside within host macrophages and form biofilm‐like communities contributes to the persistent and drug‐tolerant nature of the disease. Compounds that can prevent or reverse the biofilm‐like phenotype have the potential to serve alongside TB antibiotics to overcome this tolerance, and decrease treatment duration. Using Mycobacterium smegmatis as a surrogate organism, we report the identification of two new 2‐aminoimidazole compounds that inhibit and disperse mycobacterial biofilms, work synergistically with isoniazid and rifampicin to eradicate preformed M. smegmatis biofilms in vitro, are nontoxic toward Galleria mellonella, and exhibit stability in mouse plasma.}, number={9}, journal={CHEMMEDCHEM}, author={Nguyen, T. Vu and Minrovic, Bradley M. and Melander, Roberta J. and Melander, Christian}, year={2019}, month={May}, pages={927–937} }
 @article{nguyen_peszko_melander_melander_2019, title={Using 2-aminobenzimidazole derivatives to inhibit Mycobacterium smegmatis biofilm formation}, volume={10}, ISSN={["2040-2511"]}, DOI={10.1039/c9md00025a}, abstractNote={Biofilm formation by mycobacteria can lead to enhanced antibiotic tolerance.}, number={3}, journal={MEDCHEMCOMM}, author={Nguyen, T. Vu and Peszko, Matthew T. and Melander, Roberta J. and Melander, Christian}, year={2019}, month={Mar}, pages={456–459} }
 @article{huggins_nguyen_hahn_baker_kuo_kaur_melander_gunn_melander_2018, title={2-Aminobenzimidazoles as antibiofilm agents against Salmonella enterica serovar Typhimurium}, volume={9}, ISSN={["2040-2511"]}, DOI={10.1039/c8md00298c}, abstractNote={Serovars within the species Salmonella enterica are some of the most common food and water-borne pathogens worldwide.}, number={9}, journal={MEDCHEMCOMM}, author={Huggins, William M. and Nguyen, T. Vu and Hahn, Nicholas A. and Baker, James T. and Kuo, Laura G. and Kaur, Darpan and Melander, Roberta J. and Gunn, John S. and Melander, Christian}, year={2018}, month={Sep}, pages={1547–1552} }
 @article{jeon_obregon-henao_ackart_podell_belardinelli_jackson_nguyen_blackledge_melander_melander_et al._2017, title={2-aminoimidazoles potentiate beta-lactam antimicrobial activity against Mycobacterium tuberculosis by reducing beta-lactamase secretion and increasing cell envelope permeability}, volume={12}, number={7}, journal={PLoS One}, author={Jeon, A. B. and Obregon-Henao, A. and Ackart, D. F. and Podell, B. K. and Belardinelli, J. M. and Jackson, M. and Nguyen, T. V. and Blackledge, M. S. and Melander, R. J. and Melander, C. and et al.}, year={2017} }
 @article{barker_martin_chandler_nguyen_harris_goodell_melander_doi_ernst_melander_2017, title={Small molecule adjuvants that suppress both chromosomal and mcr-1 encoded colistin-resistance and amplify colistin efficacy in polymyxin-susceptible bacteria}, volume={25}, ISSN={["1464-3391"]}, DOI={10.1016/j.bmc.2017.08.055}, abstractNote={Bacterial resistance to polymyxin antibiotics has taken on a new and more menacing form. Common are genomically-encoded resistance mechanisms to polymyxins, specifically colistin (polymyxin E), however, the plasmid-borne mobile colistin resistance-1 (mcr-1) gene has recently been identified and poses a new threat to global public health. Within six months of initial identification in Chinese swine in November 2015, the first human clinical isolation in the US was reported (Apr. 2016). Herein we report successful reversion of mcr-1-driven colistin resistance in Acinetobacter baumannii, Klebsiella pneumoniae, and Escherichia coli with adjuvants we previously reported as modulators of chromosomally-encoded colistin resistance. Further screening of our in-house library of nitrogen-dense heterocycles has identified additional chemical scaffolds that actively attenuate colistin resistance. Ultimately, we present a diverse cohort of adjuvants that both sensitize colistin-resistant and colistin-susceptible bacteria to this antibiotic, thus providing a potential avenue to both reduce colistin dosage and toxicity, and overcome colistin resistance.}, number={20}, journal={BIOORGANIC & MEDICINAL CHEMISTRY}, author={Barker, William T. and Martin, Sara E. and Chandler, Courtney E. and Nguyen, T. Vu. and Harris, Tyler L. and Goodell, Christopher and Melander, Roberta J. and Doi, Yohei and Ernst, Robert K. and Melander, Christian}, year={2017}, month={Oct}, pages={5749–5753} }
 @article{nguyen_blackledge_lindsey_minrovic_ackart_jeon_obregon-henao_melander_basaraba_melander_2017, title={The Discovery of 2-Aminobenzimidazoles That Sensitize Mycobacterium smegmatis and M. tuberculosis to beta-Lactam Antibiotics in a Pattern Distinct from beta-Lactamase Inhibitors}, volume={56}, ISSN={["1521-3773"]}, DOI={10.1002/anie.201612006}, abstractNote={AbstractA library of 2‐aminobenzimidazole derivatives was screened for the ability to suppress β‐lactam resistance in Mycobacterium smegmatis. Several non‐bactericidal compounds were identified that reversed intrinsic resistance to β‐lactam antibiotics in a manner distinct from β‐lactamase inhibitors. Activity also translates to M. tuberculosis, with a lead compound from this study potently suppressing carbenicillin resistance in multiple M. tuberculosis strains (including multidrug‐resistant strains). Preliminary mechanistic studies revealed that the lead compounds act through a mechanism distinct from that of traditional β‐lactamase inhibitors.}, number={14}, journal={ANGEWANDTE CHEMIE-INTERNATIONAL EDITION}, author={Nguyen, T. Vu and Blackledge, Meghan S. and Lindsey, Erick A. and Minrovic, Bradley M. and Ackart, David F. and Jeon, Albert B. and Obregon-Henao, Andres and Melander, Roberta J. and Basaraba, Randall J. and Melander, Christian}, year={2017}, month={Mar}, pages={3940–3944} }