Design, synthesis, and biological activity of potent and selective inhibitors of mast cell tryptase

Corey R Hopkins; Mark Czekaj; Steven S Kaye; Zhongli Gao; James Pribish; Henry Pauls; Guyan Liang; Keith Sides; Dona Cramer; Jennifer Cairns; Yongyi Luo; Heng-Keang Lim; Roy Vaz; Sam Rebello; Sebastian Maignan; Alain Dupuy; Magali Mathieu; Julian Levell

doi:10.1016/j.bmcl.2005.04.002

Design, synthesis, and biological activity of potent and selective inhibitors of mast cell tryptase

Bioorg Med Chem Lett. 2005 Jun 2;15(11):2734-7. doi: 10.1016/j.bmcl.2005.04.002.

Authors

Corey R Hopkins¹, Mark Czekaj, Steven S Kaye, Zhongli Gao, James Pribish, Henry Pauls, Guyan Liang, Keith Sides, Dona Cramer, Jennifer Cairns, Yongyi Luo, Heng-Keang Lim, Roy Vaz, Sam Rebello, Sebastian Maignan, Alain Dupuy, Magali Mathieu, Julian Levell

Affiliation

¹ Department of Medicinal Chemistry, Aventis Pharmaceuticals, Bridgewater, NJ 08807, USA. corey.hopkins@aventis.com

PMID: 15911249
DOI: 10.1016/j.bmcl.2005.04.002

Abstract

A new series of novel mast cell tryptase inhibitors is reported, which features the use of an indole structure as the hydrophobic substituent on a m-benzylaminepiperidine template. The best members of this series display good in vitro activity and excellent selectivity against other serine proteases.

MeSH terms

Enzyme Inhibitors / chemical synthesis*
Enzyme Inhibitors / chemistry
Enzyme Inhibitors / pharmacology*
Mast Cells / enzymology*
Models, Molecular
Serine Endopeptidases / drug effects*
Structure-Activity Relationship
Tryptases

Substances

Enzyme Inhibitors
Serine Endopeptidases
Tryptases