Boric acid and acetate anion binding to subclass B3 metallo-β-lactamase BJP-1 provides clues for mechanism of action and inhibitor design

Di Pisa, F.; Pozzi, C.; Benvenuti, M.; Docquier, Jean-Denis; De Luca, F.; Mangani, S.

doi:10.1016/j.ica.2017.07.030

Article (Scientific journals)

Boric acid and acetate anion binding to subclass B3 metallo-β-lactamase BJP-1 provides clues for mechanism of action and inhibitor design

Di Pisa, F.; Pozzi, C.; Benvenuti, M. et al.

2018 • In Inorganica Chimica Acta, 470, p. 331-341

Peer Reviewed verified by ORBi

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https://hdl.handle.net/2268/252549

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10.1016/j.ica.2017.07.030

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Keywords :

Antibiotic resistance; Inhibitor; Metallo β-lactamase; Subclass B3; X-ray crystallography; Antibiotics; Boric acid; Crystal atomic structure; Enzymes; Health risks; Molecules; X ray analysis; X rays; Zinc compounds; Bacterial resistance; Lactamases; Microbial infections; Risk to human health; Small molecule inhibitor; X ray crystallography

Abstract :

[en] Microbial infections represent a major risk to human health. In this respect, β-lactam antibiotics constitute a key therapeutic resource against such infections. However, we are facing increasing microbial resistance to antibiotic treatment and particularly worrisome is the emergence of resistant bacterial strains towards β-lactam antibiotics that can rapidly disseminate worldwide. β-lactamase enzymes are the main determinant of bacterial resistance and among them metallo-β-lactamases (MBLs) are most threatening, as exemplified by the recent resistance outbreaks due to New Delhi β-lactamase 1 (NDM-1) producing bacteria. MBLs are mono or di-zinc enzymes able to inactivate clinically important β-lactam antibiotics including carbapenems, which are used as a last resort therapy in severe infections. Under this scenery, the discovery of new potent inhibitors of MBLs becomes an urgent need and X-ray crystallography of MBLs in complex with small molecule inhibitors provides the possibility to accelerate the process of drug discovery. We present here the atomic-resolution crystal structures of BJP-1, a di-zinc MBL, in complex with two small molecules and their comparison with other MBL complexes with inhibitors. These structural data, besides providing hints about the mechanism of di-zinc MBLs, might be the starting point for a fragment-based lead-discovery program. © 2017 Elsevier B.V.

Disciplines :

Biochemistry, biophysics & molecular biology
Microbiology

Author, co-author :

Di Pisa, F.; Department of Biotechnology, Chemistry and Pharmacy, University of Siena, Siena, 53100, Italy

Pozzi, C.; Department of Biotechnology, Chemistry and Pharmacy, University of Siena, Siena, 53100, Italy

Benvenuti, M.; Department of Biotechnology, Chemistry and Pharmacy, University of Siena, Siena, 53100, Italy

Docquier, Jean-Denis ; Université de Liège - ULiège > Département des sciences de la vie > Centre d'ingénierie des protéines

De Luca, F.; Department of Medical Biotechnology, University of Siena53100, Italy

Mangani, S.; Department of Biotechnology, Chemistry and Pharmacy, University of Siena, Siena, 53100, Italy, Magnetic Resonance Center CERM, University of Florence, Sesto Fiorentino (Fi), 50019, Italy

Language :

English

Title :

Boric acid and acetate anion binding to subclass B3 metallo-β-lactamase BJP-1 provides clues for mechanism of action and inhibitor design

Publication date :

2018

Journal title :

Inorganica Chimica Acta

ISSN :

0020-1693

Publisher :

Elsevier S.A.

Volume :

470

Pages :

331-341

Peer reviewed :

Peer Reviewed verified by ORBi

Available on ORBi :

since 13 November 2020

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