Design, synthesis, and biological activity of potent and selective inhibitors of mast cell tryptase.
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.
Hopkins
Corey R
CR
Department of Medicinal Chemistry, Aventis Pharmaceuticals, Bridgewater, NJ 08807, USA. corey.hopkins@aventis.com
Czekaj
Mark
M
Kaye
Steven S
SS
Gao
Zhongli
Z
Pribish
James
J
Pauls
Henry
H
Liang
Guyan
G
Sides
Keith
K
Cramer
Dona
D
Cairns
Jennifer
J
Luo
Yongyi
Y
Lim
Heng-Keang
HK
Vaz
Roy
R
Rebello
Sam
S
Maignan
Sebastian
S
Dupuy
Alain
A
Mathieu
Magali
M
Levell
Julian
J
D004791:Enzyme Inhibitors / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology*; D008407:Mast Cells / Q000201:enzymology*; D008958:Models, Molecular; D012697:Serine Endopeptidases / Q000187:drug effects*; D013329:Structure-Activity Relationship; D053802:Tryptases
D004791:Enzyme Inhibitors; D012697:Serine Endopeptidases; D053802:Tryptases