A small library of peptide amides was designed to profile the cathepsin L active site. Within
the cathepsin family of cysteine proteases, the first round of selection was on cathepsin L …

By screening a combinatorial pentapeptide amide collection in an inhibition assay, we
systematically evaluated the potential of 19 proteinogenic amino acids and seven …

A novel series of noncovalent inhibitors of cathepsin L have been designed to mimic the
mode of autoinhibition of procathepsin L. Just like the propeptide, these peptide-based …

The extension of a previously reported cathepsin K azepanone-based inhibitor template to
the design and synthesis of potent and selective inhibitors of the homologous cysteine …

We report a series of noncovalent, reversible inhibitors of cathepsin L that have been
designed to explore additional binding interactions with the S′ subsites. The design was …

The substrate activity screening (SAS) method, a substrate-based fragment identification
and optimization method for the development of enzyme inhibitors, was previously applied …

The design and synthesis of dipeptidyl disulfides and dipeptidyl benzoylhydrazones as
selective inhibitors of the cysteine protease Cathepsin S are described. These inhibitors …

We report a novel series of noncovalent inhibitors of cathepsin S. The synthesis of the
peptidomimetic scaffold is described and structure–activity relationships of P3, P1, and P1 …

We have utilized previously known substrate and inhibitor specificity profiles for the
lysosomal cysteine protease, cathepsin L, to design a new series of putative inhibitors of this …

Aberrant levels of cathepsin L (Cts L), a ubiquitously expressed endosomal cysteine
protease, have been implicated in many diseases such as cancer and diabetes …