1027309-84-7Relevant articles and documents
Poststatin, a new inhibitor of prolyl endopeptidase. V. Endopeptidase inhibitory activity of poststatin analogues
Tsuda, Makoto,Muraoka, Yasuhiko,Nagai, Machiko,Aoyagi, Takaaki,Takeuchi, Tomio
, p. 890 - 899 (2007/10/03)
Thirty analogues of poststatin were synthesized, and their inhibitory activities against prolyl endopeptidase, human leukocyte elastase and cathepsin B were measured. The α-ketone was essential and the S configuration was preferable to the R configuration in the β-substituted-β-amino-α-oxopropionic acid moiety of poststatin analogues for endopeptidase inhibitory activity. The analogue in which the D-leucine residue of poststatin was replaced by L-leucine showed strong inhibitory activity to cathepsin B. Introduction of an aromatic group into the P4 position and proline into the P2 position increased inhibitory activity to elastase. Benzyloxycarbonyl-L-homophenylalanyl-(RS)-3-amino-2-oxovaleryl-D- leucyl-L-valine was about 6 times more active to prolyl endopeptidase than natural poststatin.