636572-72-0Relevant articles and documents
Naphthyl-l-α-amino acids via chemo-enzymatic dynamic kinetic resolution
D'Arrigo, Paola,Cerioli, Lorenzo,Fiorati, Andrea,Servi, Stefano,Viani, Fiorenza,Tessaro, Davide
experimental part, p. 938 - 944 (2012/10/08)
A double catalyst system (protease + base) was applied to the dynamic kinetic resolution (DKR) of isomeric 1- and 2-α-naphthyl-glycines and -alanines exploiting the in situ racemization of their thioesters. Due to the different C-acidity of the two sets of compounds, different experimental conditions have been devised to perform the simultaneous resolution/racemization process. In all cases, the racemic N-Boc-thioesters were converted into the aminoacids with an l-configuration almost quantitatively and with complete enantioselectivity. 2012 Elsevier Ltd.
Design of plasma kallikrein inhibitors: Functional and structural requirements of plasma kallikrein inhibitors
Tsuda, Yuko,Wanaka, Keiko,Tada, Mayako,Okamoto, Shosuke,Hijikata-Okunomiya, Akiko,Okada, Yoshio
, p. 452 - 457 (2007/10/03)
The synthetic plasma kallikrein (PK) inhibitor trans-4- aminomethylcyclohexanecarbonylphenylalanine-4-carboxymethylanilide (PKSI- 527) consists of three parts. Each part was replaced by analogues in an attempt to improve the potency and the selectivity of PKSI-527. Among the peptides examined, trans-4-aminomethyl-cyclohexanecarbonylphenylalanine-4- carboxyanilide (peptide 16) inhibited PK with a high selectivity and an IC50 value of 2.7 μM, being as potent as PKSI-527.