Agricultural and biological chemistry p. 37 - 43 (1991)
Update date:2022-08-05
Topics:
Yoshimoto
Tsuru
Yamamoto
Ikezawa
Furukawa
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.
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(1991)Doi:10.1002/ejoc.201100731
(2011)Doi:10.1021/jo00013a009
(1991)Doi:10.1039/c1ob06595e
(2012)Doi:10.1002/hlca.19910740820
(1991)Doi:10.1080/00397919208021306
(1992)