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Bivalent inhibition of beta-tryptase: Distance scan of neighboring subunits by dibasic inhibitors

MPG-Autoren
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Schaschke,  N.
Moroder, Luis / Bioorganic Chemistry, Max Planck Institute of Biochemistry, Max Planck Society;

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Zitation

Schaschke, N., Dominik, A., Matschiner, G., & Sommerhoff, C. P. (2002). Bivalent inhibition of beta-tryptase: Distance scan of neighboring subunits by dibasic inhibitors. Bioorganic & Medicinal Chemistry Letters, 12(6), 985-988.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0010-6F88-5
Zusammenfassung
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 beta- tryptase tetramer. The K-i-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 experimental data are in full agreement with predictions derived from a novel modeling program that allows the docking of bivalent ligands. (C) 2002 Elsevier Science Ltd. All rights reserved.