Utilization of the 1,2,3,5-thiatriazolidin-3-one 1,1-dioxide scaffold in the design of potential inhibitors of human neutrophil proteinase 3

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Dou, Dengfeng
He, Guijia
Li, Yi
Lai, Zhong
Wei, Liuqing
Alliston, Kevin R.
Lushington, Gerald H.
Eichhorn, David M.
Groutas, William C.

Bioorganic & medicinal chemistry. 2010 Feb; 18(3): 1093-102.


The S' subsites of human neutrophil proteinase 3 (Pr 3) were probed by constructing diverse libraries of compounds based on the 1,2,3,5-thiatriazolidin-3-one 1,1-dioxide using combinational and click chemistry methods. The multiple points of diversity embodied in the heterocyclic scaffold render it well-suited to the exploration of the S' subsites of Pr 3. Molecular modeling studies suggest that further exploration of the S' subsites of Pr 3 using the aforementioned heterocyclic scaffold may lead to the identification of highly selective, reversible competitive inhibitors of Pr 3.

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