Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/150178
Title: Impact of pyridyl moieties on the inhibitory properties of prominent acyclic metal chelators against metallo-β-lactamase-producing Enterobacteriaceae : investigating the molecular basis of acyclic metal chelators' activity
Authors: Sosibo, Sphelele C.
Somboro, Anou M.
Amoako, Daniel G.
Osei Sekyere, John
Bester, Linda A.
Ngila, Jane C.
Sun, Darren Delai
Kumalo, Hezekiel M.
Keywords: Engineering::Chemical engineering
Issue Date: 2019
Source: Sosibo, S. C., Somboro, A. M., Amoako, D. G., Osei Sekyere, J., Bester, L. A., Ngila, J. C., Sun, D. D. & Kumalo, H. M. (2019). Impact of pyridyl moieties on the inhibitory properties of prominent acyclic metal chelators against metallo-β-lactamase-producing Enterobacteriaceae : investigating the molecular basis of acyclic metal chelators' activity. Microbial Drug Resistance, 25(3), 439-449. https://dx.doi.org/10.1089/mdr.2018.0272
Journal: Microbial Drug Resistance
Abstract: Carbapenem-resistant Enterobacteriaceae (CREs)-mediated infections remain a huge public health concern. CREs produce enzymes such as metallo-β-lactamases (MBLs), which inactivate β-lactam antibiotics. Hence, developing efficient molecules capable of inhibiting these enzymes remains a way forward to overcoming this phenomenon. In this study, we demonstrate that pyridyl moieties favor the inhibitory activity of cyclic metal-chelating agents through in vitro screening, molecular modeling, and docking assays. Di-(2-picolyl) amine and tris-(2-picolyl) amine exhibited great efficacy against different types of MBLs and strong binding affinity for NDM-1, whereas 2-picolyl amine did not show activity at a concentration of 64 mg/L in combination with meropenem; it further showed the lowest binding affinity from computational molecular analysis, commensurating with the in vitro screening assays. The findings revealed that the pyridyl group plays a vital role in the inhibitory activity of the tested molecules against CREs and should be exploited as potential MBL inhibitors.
URI: https://hdl.handle.net/10356/150178
ISSN: 1076-6294
DOI: 10.1089/mdr.2018.0272
Rights: © 2019 Mary Ann Liebert, Inc., publishers. All rights reserved.
Fulltext Permission: none
Fulltext Availability: No Fulltext
Appears in Collections:CEE Journal Articles

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