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Cover Picture: Upgrading a Natural Product: Inhibition of Human β‐Tryptase by Cyclotheonamide Analogues (ChemMedChem 3/2010)
Author(s) -
Schaschke Norbert,
Sommerhoff Christian P.
Publication year - 2010
Publication title -
chemmedchem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 0.817
H-Index - 100
eISSN - 1860-7187
pISSN - 1860-7179
DOI - 10.1002/cmdc.201090005
Subject(s) - tryptase , chemistry , natural product , serine protease , protease , active site , trypsin , serine , biochemistry , stereochemistry , combinatorial chemistry , computational biology , enzyme , biology , immunology , mast cell
The cover picture shows the putative binding mode of cyclotheonamide A along the active‐site cleft of subunit A of the β‐tryptase homotetramer (top), a serine protease with trypsin‐like activity that has been the focus of interest as a promising new drug target in the treatment of asthma. Based on this model, the cyclotheonamide E4 scaffold was modified in two ways (indicated in orange) to give potent and selective β‐tryptase inhibitors that bind reversibly to the protein (bottom). For more details, see the Communication by N. Schaschke and C. P. Sommerhoff on p. 367 ff.