TY  - JOUR
U1  - Zeitschriftenartikel, wissenschaftlich - begutachtet (reviewed)
A1  - Schmitz, Janina
A1  - Beckmann, Anna-Madeleine
A1  - Dudic, Adela
A1  - Li, Tianwei
A1  - Sellier, Robert
A1  - Bartz, Ulrike
A1  - Gütschow, Michael
T1  - 3-Cyano-3-aza-β-amino Acid Derivatives as Inhibitors of Human Cysteine Cathepsins
JF  - ACS Medicinal Chemistry Letters
N2  - Nitrile-type inhibitors are known to interact with cysteine proteases in a covalent-reversible manner. The chemotype of 3-cyano-3-aza-β-amino acid derivatives was designed in which the N-cyano group is centrally arranged in the molecule to allow for interactions with the nonprimed and primed binding regions of the target enzymes. These compounds were evaluated as inhibitors of the human cysteine cathepsins K, S, B, and L. They exhibited slow-binding behavior and were found to be exceptionally potent, in particular toward cathepsin K, with second-order rate constants up to 52 900 × 103 M–1 s–1.
KW  - human cathepsins
KW  - β-amino acids
KW  - cysteine proteases
KW  - nitrile inhibitors
UN  - https://nbn-resolving.org/urn:nbn:de:hbz:1044-opus-13258
SN  - 1948-5875
SS  - 1948-5875
U6  - https://doi.org/10.1021/ml500238q
DO  - https://doi.org/10.1021/ml500238q
PM  - 25313316
VL  - 5
IS  - 10
SP  - 1076
EP  - 1081
PB  - ACS Publications
ER  -