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Molecular Insights into Avibactam Mediated Class C β-Lactamase Inhibition: Competition Between Reverse Acylation and Hydrolysis Through Desulfation

Abstract

Avibactam is one of the promising next generation β-lactamase inhibitors due to its exceptional inhibition against wide-spectrum serine β-lactamases. The unusual reversible acylation mechanism has particularly gained interest to explain the inhibition mechanism of avibactam. We explore the mechanism of acylation and deacylation involving avibactam in class C β-lactamases (CBL) through hybrid quantum mechanical/molecular mechanical (QM/MM) enhanced sampling molecular dynamics (MD) simulations. Based on these computations, we probe the kinetic stability of the acyl-enzyme complex formed by avibactam and CBL, thereby gaining molecular level insights on the avibactam mediated inhibition of CBL.

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Publication details

The article was received on 14 Mar 2018, accepted on 01 May 2018 and first published on 01 May 2018


Article type: Paper
DOI: 10.1039/C8CP01670D
Citation: Phys. Chem. Chem. Phys., 2018, Accepted Manuscript
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    Molecular Insights into Avibactam Mediated Class C β-Lactamase Inhibition: Competition Between Reverse Acylation and Hydrolysis Through Desulfation

    C. K. Das and N. N. Nair, Phys. Chem. Chem. Phys., 2018, Accepted Manuscript , DOI: 10.1039/C8CP01670D

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