Now showing items 1-2 of 2

    • Metallo-β-lactamase inhibitors by bioisosteric replacement: preparation, activity and binding 

      Skagseth, Susann; Akhter, Sundus; Paulsen, Marianne H; Muhammad, Zeeshan; Samuelsen, Ørjan; Leiros, Hanna-Kirsti S.; Bayer, Annette (Journal article; Tidsskriftartikkel; Peer reviewed, 2017-04-14)
      Bacterial resistance is compromising the use of β-lactam antibiotics including carbapenems. The main resistance mechanism against β-lactams is hydrolysis of the β-lactam ring mediated by serine- or metallo-β-lactamases (MBLs). Although several inhibitors of MBLs have been reported, none has been developed into a clinically useful inhibitor. Mercaptocarboxylic acids are among the most prominent ...
    • Structural insights into TMB-1 and the role of residues 119 and 228 in substrate and inhibitor binding 

      Skagseth, Susann; Christopeit, Tony; Akhter, Sundus; Bayer, Annette; Samuelsen, Ørjan; Leiros, Hanna-Kirsti S. (Journal article; Tidsskriftartikkel; Peer reviewed, 2017-05-30)
      Metallo-β-lactamases (MBLs) threaten the effectiveness of β-lactam antibiotics, including carbapenems, and are a concern for global public health. β-Lactam/β-lactamase inhibitor combinations active against class A and class D carbapenemases are used, but no clinically useful MBL inhibitor is currently available. Tripoli metallo-β-lactamase-1 (TMB-1) and TMB-2 are members of MBL subclass B1a, where ...