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              <p>The rise of resistances in Gram negative bacteria is reaching an extremely worrying situation and one of the main causes of resistance is the massive spread of very efficient β-lactamases, which render most β-lactam antibiotics useless. Herein, we report the development of a series of imino-analogs of β-lactams (namely azetidinimines) as efficient non-covalent inhibitors of β-lactamases. Despite the structural and mechanistic differences between serine-β-lactamases KPC-2 and OXA-48 and metallo-betalactamase NDM-1, all three enzymes can be inhibited at a submicromolar level by compound 7dfm, which can also repotentiate imipenem against a resistant strain of Escherichia coli expressing NDM-1. We show that this compound can  efficiently  inhibit  not  only the  three  main  clinically-relevant  carbapenemases of  Ambler classes A, B and D, but also β-lactamases ofall four classes (A, B, C and D). Our results pave the  way  for  the  development  of  a  newstructurally  originalfamily  of  non-covalent broad-spectrum inhibitors of β-lactamases.</p>
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