de.mpg.escidoc.pubman.appbase.FacesBean
English
 
Help Guide Disclaimer Contact us Login
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

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

MPS-Authors
http://pubman.mpdl.mpg.de/cone/persons/resource/persons78621

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

Locator
There are no locators available
Fulltext (public)
There are no public fulltexts available
Supplementary Material (public)
There is no public supplementary material available
Citation

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.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-6F88-5
Abstract
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.