{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,28]],"date-time":"2026-09-28T15:33:15Z","timestamp":1790609595816,"version":"4.1.0"},"reference-count":50,"publisher":"MDPI AG","issue":"1","license":[{"start":{"date-parts":[[2021,12,22]],"date-time":"2021-12-22T00:00:00Z","timestamp":1640131200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100007137","name":"Northern Norway Regional Health Authority","doi-asserted-by":"publisher","award":["HNF1514-20"],"award-info":[{"award-number":["HNF1514-20"]}],"id":[{"id":"10.13039\/501100007137","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100016934","name":"Troms\u00f8 research foundation","doi-asserted-by":"publisher","award":["xx"],"award-info":[{"award-number":["xx"]}],"id":[{"id":"10.13039\/100016934","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecules"],"abstract":"<jats:p>Inhibition of bacterial virulence is believed to be a new treatment option for bacterial infections. In the present study, we tested dipicolylamine (DPA), tripicolylamine (TPA), tris pyridine ethylene diamine (TPED), pyridine and thiophene derivatives as putative inhibitors of the bacterial virulence factors thermolysin (TLN), pseudolysin (PLN) and aureolysin (ALN) and the human zinc metalloproteases, matrix metalloprotease-9 (MMP-9) and matrix metalloprotease-14 (MMP-14). These compounds have nitrogen or sulfur as putative donor atoms for zinc chelation. In general, the compounds showed stronger inhibition of MMP-14 and PLN than of the other enzymes, with Ki values in the lower \u03bcM range. Except for DPA, none of the compounds showed significantly stronger inhibition of the virulence factors than of the human zinc metalloproteases. TPA and Zn230 were the only compounds that inhibited all five zinc metalloproteinases with a Ki value in the lower \u03bcM range. The thiophene compounds gave weak or no inhibition. Docking indicated that some of the compounds coordinated zinc by one oxygen atom from a hydroxyl or carbonyl group, or by oxygen atoms both from a hydroxyl group and a carbonyl group, and not by pyridine nitrogen as in DPA and TPA.<\/jats:p>","DOI":"10.3390\/molecules27010056","type":"journal-article","created":{"date-parts":[[2021,12,23]],"date-time":"2021-12-23T02:01:19Z","timestamp":1640224879000},"page":"56","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":18,"title":["Zinc-Chelating Compounds as Inhibitors of Human and Bacterial Zinc Metalloproteases"],"prefix":"10.3390","volume":"27","author":[{"given":"Fatema","family":"Rahman","sequence":"first","affiliation":[{"name":"Molecular Pharmacology and Toxicology, Department of Medical Biology, Faculty of Health Sciences, UiT\u2014The Arctic University of Norway, NO-9037 Troms\u00f8, Norway"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Imin","family":"Wushur","sequence":"additional","affiliation":[{"name":"Molecular Pharmacology and Toxicology, Department of Medical Biology, Faculty of Health Sciences, UiT\u2014The Arctic University of Norway, NO-9037 Troms\u00f8, Norway"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nabin","family":"Malla","sequence":"additional","affiliation":[{"name":"Molecular Pharmacology and Toxicology, Department of Medical Biology, Faculty of Health Sciences, UiT\u2014The Arctic University of Norway, NO-9037 Troms\u00f8, Norway"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ove Alexander H\u00f8gmoen","family":"\u00c5strand","sequence":"additional","affiliation":[{"name":"Department of Pharmaceutical Chemistry, School of Pharmacy, University of Oslo, NO-0316 Oslo, Norway"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"P\u00e5l","family":"Rongved","sequence":"additional","affiliation":[{"name":"Department of Pharmaceutical Chemistry, School of Pharmacy, University of Oslo, NO-0316 Oslo, Norway"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jan-Olof","family":"Winberg","sequence":"additional","affiliation":[{"name":"Molecular Pharmacology and Toxicology, Department of Medical Biology, Faculty of Health Sciences, UiT\u2014The Arctic University of Norway, NO-9037 Troms\u00f8, Norway"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3290-3736","authenticated-orcid":false,"given":"Ingebrigt","family":"Sylte","sequence":"additional","affiliation":[{"name":"Molecular Pharmacology and Toxicology, Department of Medical Biology, Faculty of Health Sciences, UiT\u2014The Arctic University of Norway, NO-9037 Troms\u00f8, Norway"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2021,12,22]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"2507","DOI":"10.1056\/NEJMra1106700","article-title":"Proprotein convertases in health and disease","volume":"365","author":"Artenstein","year":"2011","journal-title":"N. 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