Trypsin inhibitors for the treatment of pancreatitis
- Resource Type
- Authors
- Trixi Brandl; Kenji Namoto; Frederic Berst; Irene Mueller; Philip R. Skaanderup; Julian Woelcke; Oliver Simic; Nikolaus Schiering; Claus Ehrhardt
- Source
- Bioorganic & Medicinal Chemistry Letters. 26:4340-4344
- Subject
- 0301 basic medicine
Proteases
Trypsin inhibitor
Clinical Biochemistry
hERG
Pharmaceutical Science
Crystallography, X-Ray
01 natural sciences
Biochemistry
Serine
Inhibitory Concentration 50
Structure-Activity Relationship
03 medical and health sciences
Drug Discovery
Hydrolase
medicine
Humans
Moiety
Molecular Biology
Molecular Structure
biology
Kunitz STI protease inhibitor
010405 organic chemistry
Chemistry
Organic Chemistry
Trypsin
0104 chemical sciences
Enzyme Activation
030104 developmental biology
Pancreatitis
biology.protein
Molecular Medicine
Trypsin Inhibitors
medicine.drug
- Language
- ISSN
- 0960-894X
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.