Schaschke, Norbert et al. published their research in Bioorganic & Medicinal Chemistry Letters in 2002 |CAS: 53838-27-0

The Article related to bivalent inhibitor tryptase active site stereochem, Enzymes: Substrates-Cofactors-Inhibitors-Activators-Coenzymes-Products and other aspects.SDS of cas: 53838-27-0

On March 25, 2002, Schaschke, Norbert; Dominik, Andreas; Matschiner, Gabriele; Sommerhoff, Christian P. published an article.SDS of cas: 53838-27-0 The title of the article was Bivalent inhibition of β-Tryptase: distance scan of neighboring subunits by dibasic inhibitors. And the article contained the following:

Based on bifunctional diketopiperazines as templates and m-aminomethyl-phenylalanine as arginine mimetic, we have synthesized a new class of structurally related dibasic tryptase inhibitors with systematically increasing spacer length. These compounds were used to scan the distance between the active sites of two neighboring subunits of the β-tryptase tetramer. The Ki-values obtained are a function of the distance between the terminal amino groups and indicate optimal binding of inhibitors with 29-31 bonds between the amino groups. These exptl. data are in full agreement with predictions derived from a novel modeling program that allows the docking of bivalent ligands. The experimental process involved the reaction of (S)-5-tert-Butyl 1-methyl 2-aminopentanedioate(cas: 53838-27-0).SDS of cas: 53838-27-0

The Article related to bivalent inhibitor tryptase active site stereochem, Enzymes: Substrates-Cofactors-Inhibitors-Activators-Coenzymes-Products and other aspects.SDS of cas: 53838-27-0

Referemce:
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