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Bioorg Med Chem Lett. 2016 Aug 1;26(15):3741-5. doi: 10.1016/j.bmcl.2016.05.071. Epub 2016 May 26.

Evaluation of bisbenzamidines as inhibitors for matriptase-2.

Author information

1
Pharmaceutical Institute, Pharmaceutical Chemistry I, University of Bonn, An der Immenburg 4, 53121 Bonn, Germany.
2
Pharmaceutical Institute, Pharmaceutical Chemistry I, University of Bonn, An der Immenburg 4, 53121 Bonn, Germany; Department of Life Science Informatics, B-IT, LIMES Program Unit Chemical Biology and Medicinal Chemistry, University of Bonn, Dahlmannstr. 2, 53113 Bonn, Germany.
3
Department of Basic Pharmaceutical Science, College of Pharmacy, Xavier University of Louisiana, 1 Drexel Drive, New Orleans, LA 70125, USA.
4
Department of Life Science Informatics, B-IT, LIMES Program Unit Chemical Biology and Medicinal Chemistry, University of Bonn, Dahlmannstr. 2, 53113 Bonn, Germany.

Abstract

The serine protease matriptase-2 has attracted much attention as a potential target for the treatment of iron overload diseases. In this study, a series of 27 symmetric, achiral bisbenzamidines was evaluated for inhibitory activity against human matriptase-2, against the closely related enzyme human matriptase, as well as against human thrombin, bovine factor Xa and human trypsin. The conformationally restricted piperazine derivative 19 and the oxamide-derived bisbenzamidine 1 were identified as the most potent inhibitors of this series for matriptase-2 and matriptase, respectively.

KEYWORDS:

Bisbenzamidines; Matriptase-2; Serine proteases

PMID:
27287367
DOI:
10.1016/j.bmcl.2016.05.071
[Indexed for MEDLINE]

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