130274-70-3Relevant academic research and scientific papers
β-Sultams exhibit discrete binding preferences for diverse bacterial enzymes with nucleophilic residues
Kolb, Roman,Bach, Nina C.,Sieber, Stephan A.
supporting information, p. 427 - 429 (2014/01/06)
β-Sultams are potent electrophiles that modify nucleophilic residues in selected enzyme active sites. We here identify and characterize some of the specific bacterial targets and show a unique inhibition of the azoreductase family.
Disruption of oligomerization and dehydroalanine formation as mechanisms for ClpP protease inhibition
Gersch, Malte,Kolb, Roman,Alte, Ferdinand,Groll, Michael,Sieber, Stephan A.
supporting information, p. 1360 - 1366 (2014/02/14)
Over 100 protease inhibitors are currently used in the clinics, and most of them use blockage of the active site for their mode of inhibition. Among the protease drug targets are several enzymes for which the correct multimeric assembly is crucial to thei
Properties and Reactions of Substituted 1,2-Thiazetidine 1,1-Dioxides: Acylation of β-Sultams at C-4, Reduction of 4-Acyl-β-sultams, and Stereochemistry of 4-(α-Hydroxyalkyl)-β-sultams
Mueller, Martin,Otto, Hans-Hartwig
, p. 171 - 178 (2007/10/02)
Acylation of N-silylated and 2,3-substituted 1,2-thiazetidine 1,1-dioxides (β-sultams) results in the formation of 4-acylated β-sultams 2 and 8.The desilylation of 2 to 3 is easily done with TBAF either on silica gel or in ethanolic solution.The acylated
