134591-59-6Relevant academic research and scientific papers
Structure activity relationship of inhibitors specific for prolyl endopeptidase.
Yoshimoto,Tsuru,Yamamoto,Ikezawa,Furukawa
, p. 37 - 43 (2007/10/02)
Structural requirements of N-blocked L-proline derivatives as specific inhibitors for prolyl endopeptidase were investigated using a series of substrate analogs. Replacement of L-proline by its D-isomer remarkably reduced the inhibition. Introduction of a sulfur atom in proline and/or in the penultimate pyrrolidine rings significantly increased the inhibition, but the introduction of oxygen rather diminished the activity. A peptide linkage (acid-amide bond) between the proline and the pyrrolidine ring was also required to keep the inhibitory activity. A benzyloxycarbonyl group was most effective as an N-blocked component of the inhibitors.
