Trypsin inhibitors for the treatment of pancreatitis

[Display omitted] 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...

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Veröffentlicht in:	Bioorganic & medicinal chemistry letters 2016-09, Vol.26 (17), p.4340-4344
Hauptverfasser:	Brandl, Trixi, Simic, Oliver, Skaanderup, Philip R., Namoto, Kenji, Berst, Frederic, Ehrhardt, Claus, Schiering, Nikolaus, Mueller, Irene, Woelcke, Julian
Format:	Artikel
Sprache:	eng
Schlagworte:	Crystallography, X-Ray Enzyme Activation - drug effects hERG inhibition Humans Inhibitory Concentration 50 Molecular Structure Pancreatitis Pancreatitis - drug therapy Structure-Activity Relationship Trypsin inhibitor Trypsin Inhibitors - chemical synthesis Trypsin Inhibitors - chemistry Trypsin Inhibitors - pharmacology Trypsin Inhibitors - therapeutic use X-ray crystal structure
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