1249977-19-2Relevant articles and documents
New cathepsin inhibitors to explore the fluorophilic properties of the S2 pocket of cathepsin B: Design, synthesis, and biological evaluation
Fustero, Santos,Rodrigo, Vanessa,Sanchez-Rosello, Maria,Del Pozo, Carlos,Timoneda, Joaquin,Frizler, Maxim,Sisay, Mihiret T.,Bajorath, Juergen,Calle, Luis P.,Canada, F. Javier,Jimenez-Barbero, Jesas,Guetschow, Michael
, p. 5256 - 5260 (2011)
Fluor-in or out? Based on β,β-difluorinated cycloaliphatic amino acids, a library of new dipeptide nitriles was evaluated as human cathepsin inhibitors. The orientation of the fluorinated face relative to the protein structure of cathepsin B was elucidated by molecular modeling and NMR studies (see figure). For (R)-configured eutomers, the fluorine atoms are directed to the S2 pocket, whereas in (S)-configured distomers, the fluorinated face is solvent-exposed.
