Abstract
Kallikrein-related peptidase 6 (KLK6) is a secreted
serine protease that belongs to the family of tissue kallikreins. Aberrant
expression of KLK6 has been found in different cancers and neurodegenerative
diseases, and KLK6 is currently studied as a potential target in these pathologies.
We report a novel series of KLK6 inhibitors discovered in a high-throughput
screen within the European Lead Factory program. Structure-guided design based
on docking studies enabled rapid progression of a hit cluster to inhibitors
with improved potency, selectivity and pharmacokinetic properties. In
particular, inhibitors 32 and 34 have single digit nanomolar potency
against KLK6, with over 25-fold and 100-fold selectivity, respectively, against
the closely related enzyme trypsin. The most potent compound, 32, effectively reduces KLK6-dependent
invasion of HCT116 cells. The high potency in combination with good solubility
and low clearance of 32 make it a
good chemical probe for KLK6 target validation in vitro and potentially in
vivo.