Structural highlights
Publication Abstract from PubMed
Proline-based trypsin inhibitors occupying the S1-S2-S1' region were identified by an HTS screening campaign. It was discovered that truncation of the P1' moiety and appropriate extension into the S4 region led to highly potent trypsin inhibitors with excellent selectivity against related serine proteases and a favorable hERG profile.
Trypsin inhibitors for the treatment of pancreatitis.,Brandl T, Simic O, Skaanderup PR, Namoto K, Berst F, Ehrhardt C, Schiering N, Mueller I, Woelcke J Bioorg Med Chem Lett. 2016 Jul 17. pii: S0960-894X(16)30742-9. doi:, 10.1016/j.bmcl.2016.07.029. PMID:27476144[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Brandl T, Simic O, Skaanderup PR, Namoto K, Berst F, Ehrhardt C, Schiering N, Mueller I, Woelcke J. Trypsin inhibitors for the treatment of pancreatitis. Bioorg Med Chem Lett. 2016 Jul 17. pii: S0960-894X(16)30742-9. doi:, 10.1016/j.bmcl.2016.07.029. PMID:27476144 doi:http://dx.doi.org/10.1016/j.bmcl.2016.07.029
