Structural highlights
Publication Abstract from PubMed
Anabaenopeptins isolated from cyanobacteria were identified as inhibitors of carboxypeptidase TAFIa. Cocrystal structures of these macrocyclic natural product inhibitors in a modified porcine carboxypeptidase B revealed their binding mode and provided the basis for the rational design of small molecule inhibitors with a previously unknown central urea motif. Optimization based on these design concepts allowed for a rapid evaluation of the SAR and delivered potent small molecule inhibitors of TAFIa with a promising overall profile.
Novel Small Molecule Inhibitors of Activated Thrombin Activatable Fibrinolysis Inhibitor (TAFIa) from Natural Product Anabaenopeptin.,Halland N, Bronstrup M, Czech J, Czechtizky W, Evers A, Follmann M, Kohlmann M, Schiell M, Kurz M, Schreuder HA, Kallus C J Med Chem. 2015 May 20. PMID:25990761[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Halland N, Bronstrup M, Czech J, Czechtizky W, Evers A, Follmann M, Kohlmann M, Schiell M, Kurz M, Schreuder HA, Kallus C. Novel Small Molecule Inhibitors of Activated Thrombin Activatable Fibrinolysis Inhibitor (TAFIa) from Natural Product Anabaenopeptin. J Med Chem. 2015 May 20. PMID:25990761 doi:http://dx.doi.org/10.1021/jm501840b
