20921-11-3Relevant articles and documents
Novel chromogenic aminopeptidase substrates for the detection and identification of clinically important microorganisms
Cellier, Marie,James, Arthur L.,Orenga, Sylvain,Perry, John D.,Rasul, Ari K.,Robinson, Shaun N.,Stanforth, Stephen P.
, p. 5249 - 5269 (2014)
A series of amino acid derivatives 8-10, 42 and 43 have been prepared as chromogenic enzyme substrates in order to detect aminopeptidase activity in clinically important Gram-negative and Gram-positive bacteria. Enzymatic hydrolysis liberates the amino ac
Benzophenone Dicarboxylic Acid Antagonists of Leukotriene B4. 1. Structure-Activity Relationships of the Benzophenone Nucleus
Gapinski, D. Mark,Mallett, Barbara E.,Froelich, Larry L.,Jackson, William T.
, p. 2798 - 2807 (2007/10/02)
A series of lipophilic benzophenone dicarboxylic acid derivatives was prepared which inhibited the binding of the potent chemotaxin leukotriene B4 to its receptor(s) on intact human neutrophils.With a radioligand-binding assay as a measure of receptor affinity, a structure-activity relationship for this series was investigated.Both acidic residues were required for receptor-binding activity.The relative orientation of the two acidic groups was important for optimal binding.Replacement of the carbonyl group of the benzophenone with a variety of polar and nonpolar linking groups lead to only small changes in binding affinity, indicating the linking group may not be involved in receptor recognition.Further structure-activity relationships within this series are reported in an accompanying paper.
