Trypsin inhibitors for the treatment of pancreatitis

Bioorg Med Chem Lett. 2016 Sep 1;26(17):4340-4. doi: 10.1016/j.bmcl.2016.07.029. Epub 2016 Jul 17.


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.

Keywords: Pancreatitis; Trypsin inhibitor; X-ray crystal structure; hERG inhibition.

MeSH terms

  • Crystallography, X-Ray
  • Enzyme Activation / drug effects
  • Humans
  • Inhibitory Concentration 50
  • Molecular Structure
  • Pancreatitis / drug therapy*
  • Structure-Activity Relationship
  • Trypsin Inhibitors / chemical synthesis*
  • Trypsin Inhibitors / chemistry
  • Trypsin Inhibitors / pharmacology
  • Trypsin Inhibitors / therapeutic use*


  • Trypsin Inhibitors