Skip Navigation

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Tsuru, D.
Right arrow Articles by Furukawa, S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Tsuru, D.
Right arrow Articles by Furukawa, S.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

J. Biochem, 1988, Vol. 104, No. 4 580-586
© 1988 Japanese Biochemical Society

research-article

Thiazolidine Derivatives as Potent Inhibitors Specific for Pro1yl Endopeptidase1

Daisuke Tsuru, Tadashi Yoshimoto, Nobuhiro Koriyama and Sunao Furukawa

School of Pharmaceutical Sciences, Nagasaki University Nagasaki, Nagasaki 852

A series of N-blocked L-proline-containing compounds and their derivatives were synthesized.Their inhibitory activities for prolyl endopeptidase from bovine brain were examined and compared with that of N-benzyloxycarbonyl-L-prolyl-L-prolinal, which is the most effective enzyme inhibitor hitherto reported. Introduction of a sulfur atom into pyrrolidine ring quite effectively increased the inhibitory activity: replacement of pyrrolidine with thiazolidine or thiazolidine aldehyde (thioprolinal) and conversion of L-proline to L-thioproline residue resulted in increase in the inhibitory activity. Thus, N-benzyloxycarbonyl-L-thioprolyl-thiazolidine (Z-Thiopro-thiazolidine) and Z-LThiopro-L-thioprolinal showed K1 values of 0.36 and 0.01 nM, respectively, for prolyl endovevtidase from bovine brain; both values were significantly lower than that of Z-pro-prolinal(k1,3.7 nM).

1This work was supported in part by grants from the Ministry of Education, Science and Culture of Japan, the Research Foundation for Pharmaceutical Sciences, and the Mishima Memorial Foundation.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
A. Serizawa, P. M. Dando, and A. J. Barrett
Characterization of a Mitochondrial Metallopeptidase Reveals Neurolysin as a Homologue of Thimet Oligopeptidase
J. Biol. Chem., February 3, 1995; 270(5): 2092 - 2098.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.