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dc.contributor.authorRahman, Fatema
dc.contributor.authorNguyen, Tra-Mi
dc.contributor.authorAdekoya, Olayiwola
dc.contributor.authorCampestre, Cristina
dc.contributor.authorTortorella, Paolo
dc.contributor.authorSylte, Ingebrigt
dc.contributor.authorWinberg, Jan-Olof
dc.date.accessioned2021-08-04T06:23:11Z
dc.date.available2021-08-04T06:23:11Z
dc.date.issued2021-03-23
dc.description.abstractCompounds 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. Docking indicated that the inhibitors bound MMP-9 and MMP-14 with the phenyl, biphenyl, chlorophenyl, nitrophenyl or methoxyphenyl ringsystem in the S<sub>1</sub>′-subpocket, while these ringsystems entered the S<sub>2</sub>′- or S<sub>1</sub> -subpockets or a region involving amino acids in the S<sub>1</sub>′- and S<sub>2</sub>′-subpockets of the bacterial enzymes. An arginine conserved among the bacterial enzymes seemed to hinder entrance deeply into the S<sub>1</sub>′-subpocket. Only the bisphosphonate containing compound RC2 bound stronger to PLN and TLN than to MMP-9 and MMP-14. Docking indicated that the reason was that the conserved arginine (R203 in TLN and R198 in PLN) interacts with phosphate groups of RC2.en_US
dc.identifier.citationRahman F, Nguyen T, Adekoya OA, Campestre, Tortorella, Sylte IS, Winberg J-O. Inhibition of bacterial and human zinc metalloproteases by bisphosphonate- and catechol-containing compounds. Journal of Enzyme Inhibition and Medicinal Chemistry. 2021;36(1):819-830en_US
dc.identifier.cristinIDFRIDAID 1906704
dc.identifier.doihttps://doi.org/10.1080/14756366.2021.1901088
dc.identifier.issn1475-6366
dc.identifier.issn1475-6374
dc.identifier.urihttps://hdl.handle.net/10037/21906
dc.language.isoengen_US
dc.publisherTaylor & Francisen_US
dc.relation.ispartofRahman, F.A. (2023). Zinc binding and chelating compounds as inhibitors of bacterial metalloproteases and human matrix metalloproteases. (Doctoral thesis). <a href=https://hdl.handle.net/10037/31269>https://hdl.handle.net/10037/31269</a>.
dc.relation.journalJournal of Enzyme Inhibition and Medicinal Chemistry
dc.rights.accessRightsopenAccessen_US
dc.rights.holderCopyright 2021 The Author(s)en_US
dc.subjectVDP::Medical disciplines: 700::Basic medical, dental and veterinary science disciplines: 710::Medical biochemistry: 726en_US
dc.subjectVDP::Medisinske Fag: 700::Basale medisinske, odontologiske og veterinærmedisinske fag: 710::Medisinsk biokjemi: 726en_US
dc.titleInhibition of bacterial and human zinc-metalloproteases by bisphosphonate- and catechol-containing compoundsen_US
dc.type.versionpublishedVersionen_US
dc.typeJournal articleen_US
dc.typeTidsskriftartikkelen_US
dc.typePeer revieweden_US


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