1027162-01-1Relevant academic research and scientific papers
Structure-inhibitory activity relationship of plasmin and plasma kallikrein inhibitors
Tsuda,Tada,Wanaka,Okamoto,Hijikata-okunomiya,Okamoto,Okada
, p. 1457 - 1463 (2007/10/03)
Based on the structure of Tra-Tyr(O-Pic)-octylamide, a portion of the octylamine was replaced with moieties bearing hydrophobic, basic or acidic groups. Replacement of the C-terminal residue with a moiety bearing a hydrophobic group gave the proper affinity of the inhibitor to both plasmin (PL) and plasma kallikrein (PK). While addition of a basic residue did not improve the affinity of the inhibitor, a carboxylic acid attached to the phenyl ring increased the PK selectivity of the inhibitor.
