91650-00-9Relevant academic research and scientific papers
Design, synthesis, and in vitro evaluation of inhibitors of human leukocyte elastase based on a functionalized cyclic sulfamide scaffold
Zhong, Jiaying,Gan, Xiangdong,Alliston, Kevin R.,Groutas, William C.
, p. 589 - 593 (2007/10/03)
The design of novel functionalized templates capable of binding to the active site of serine proteases could potentially lead to the development of potent and highly selective non-covalent inhibitors of these enzymes. Using the elastase-turkey ovomucoid inhibitor complex and insights gained from earlier work based on the 1,2,5-thiadiazolidin-3-one 1,1 dioxide scaffold (I), a surrogate cyclosulfamide scaffold (II) was used for the first time in the design of reversible inhibitors of human leukocyte elastase. Compounds 7 and 8 were found to be micromolar reversible inhibitors of the enzyme.
Noncovalent inhibitors of human leukocyte elastase based on the 4-imidazolidinone scaffold
Wei, Liuqing,Gan, Xiangdong,Zhong, Jiaying,Alliston, Kevin R.,Groutas, William C.
, p. 5149 - 5153 (2007/10/03)
A central problem associated with the design of enzyme inhibitors in general, and serine protease inhibitors in particular, is the identification of templates capable of binding to the active site of an enzyme in a predictable and substrate-like fashion, orienting appended recognition elements in a correct spatial relationship so that favorable binding interactions with multiple sites are achieved. Described herein for the first time is the design of noncovalent inhibitors of human leukocyte elastase that employs a functionalized 4-imidazolidinone scaffold.
