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Influence of the Scyphostatin Side Chain on the Mode of Inhibition of Neutral Sphingomyelinase
Author(s) -
Wascholowski Veit,
Giannis Athanassios,
Pitsinos Emmanuel N.
Publication year - 2006
Publication title -
chemmedchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.817
H-Index - 100
eISSN - 1860-7187
pISSN - 1860-7179
DOI - 10.1002/cmdc.200600099
Subject(s) - novelty , sphingomyelin , focus (optics) , computational biology , computer science , chemistry , biochemistry , biology , psychology , physics , membrane , optics , social psychology
The combination of structural novelty and significant biological activity has made scyphostatin the focus of many synthetic efforts and the prototype for novel N‐SMase inhibitors. Potent, specific inhibitors of these enzymes may be valuable in deciphering their biological role and lead to the development of novel therapeutics. Scyphostatin and kotylostatin, although structurally related, exhibit different modes of inhibition towards N‐SMase.