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Cover Picture: Silanediol Protease Inhibitors: From Conception to Validation (Eur. J. Org. Chem. 2/2006)
Author(s) -
Sieburth Scott McN.,
Chen ChienAn
Publication year - 2006
Publication title -
european journal of organic chemistry
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 0.825
H-Index - 155
eISSN - 1099-0690
pISSN - 1434-193X
DOI - 10.1002/ejoc.200690004
Subject(s) - thermolysin , chemistry , chlorobenzene , protease , reagent , enzyme , silicon , cover (algebra) , stereochemistry , combinatorial chemistry , organic chemistry , catalysis , trypsin , mechanical engineering , engineering
The cover picture shows the pathway of silicon from its natural source to an organosilane protease inhibitor. Nearly all silicon exists in the form of silica, commonly encountered as sand. Silica is reduced to silicon, some becoming computer chips and some converted to organosilanes using the Müller‐Rochow (Direct) Process, which transforms chloromethane and chlorobenzene to methyl‐ and phenyl‐substituted chlorosilanes, respectively. When the two small, commercially available reagents at the bottom of the picture are subjected to a sequence of chemical reactions, they are converted into the three silanediol‐based peptide mimics at the top, which are nanomolar inhibitors of the three enzymes angiotensin‐converting enzyme (ACE), HIV protease, and thermolysin (left to right). Details are presented in the Microreview by S. McN. Sieburth and C.‐A. Chen on page 311 ff.