• Inhibition of bacterial and human zinc-metalloproteases by bisphosphonate- and catechol-containing compounds 

      Rahman, Fatema; Nguyen, Tra-Mi; Adekoya, Olayiwola; Campestre, Cristina; Tortorella, Paolo; Sylte, Ingebrigt; Winberg, Jan-Olof (Journal article; Tidsskriftartikkel; Peer reviewed, 2021-03-23)
      Compounds containg catechol or bisphosphonate were tested as inhibitors of the zinc metalloproteases, thermolysin (TLN), pseudolysin (PLN) and aureolysin (ALN) which are bacterial virulence factors, and the human matrix metalloproteases MMP-9 and −14. Inhibition of virulence is a putative strategy in the development of antibacterial drugs, but the inhibitors should not interfere with human enzymes. ...
    • The selectivity of galardin and an azasugar-based hydroxamate compound for human Matrix metalloproteases and bacterial metalloproteases 

      Sylte, Ingebrigt; Dawadi, Rangita; Malla, Nabin; von Hofsten, Susannah; Nguyen, Tra-Mi; Solli, Ann Iren; Berg, Eli; Adekoya, Olayiwola A.; Svineng, Gunbjørg; Winberg, Jan-Olof (Journal article; Tidsskriftartikkel; Peer reviewed, 2018-08-03)
      Inhibitors targeting bacterial enzymes should not interfere with enzymes of the host, and knowledge about structural determinants for selectivity is important for designing inhibitors with a therapeutic potential. We have determined the binding strengths of two hydroxamate compounds, galardin and compound 1b for the bacterial zinc metalloproteases, thermolysin, pseudolysin and auerolysin, known to ...