149268-06-4Relevant articles and documents
Metal-halogen exchange between hydrazine polyanions and α,α′-dibromo-o-xylene
Lebedev, Oleg,Maeeorg, Uno
, p. 188 - 193 (2014/02/14)
Aromatic-bridged bis(hydrazines) were found to be the main products in the reaction of hydrazine polyanions with α,α′-dibromo-o-xylene. It was confirmed that the reaction is driven by a metal-halogen exchange process. A three-step reaction mechanism is suggested.
Falcipain inhibitors: Optimization studies of the 2-pyrimidinecarbonitrile lead series
Coterón, Jose M.,Catterick, David,Castro, Julia,Chaparro, María J.,Díaz, Beatriz,Fernández, Esther,Ferrer, Santiago,Gamo, Francisco J.,Gordo, Mariola,Gut, Jiri,De Las Heras, Laura,Legac, Jennifer,Marco, Maria,Miguel, Juan,Mu?oz, Vicente,Porras, Esther,De La Rosa, Juan C.,Ruiz, Jose R.,Sandoval, Elena,Ventosa, Pilar,Rosenthal, Philip J.,Fiandor, Jose M.
experimental part, p. 6129 - 6152 (2010/10/21)
Falcipain-2 and falcipain-3 are papain-family cysteine proteases of the malaria parasite Plasmodium falciparum that are responsible for host hemoglobin hydrolysis to provide amino acids for parasite protein synthesis. Different heteroarylnitrile derivatives were studied as potential falcipain inhibitors and therefore potential antiparasitic lead compounds, with the 5-substituted-2- cyanopyrimidine chemical class emerging as the most potent and promising lead series. Through a sequential lead optimization process considering the different positions present in the initial scaffold, nanomolar and subnanomolar inhibitors at falcipains 2 and 3 were identified, with activity against cultured parasites in the micromolar range. Introduction of protonable amines within lead molecules led to marked improvements of up to 1000 times in activity against cultured parasites without noteworthy alterations in other SAR tendencies. Optimized compounds presented enzymatic activities in the picomolar to low nanomolar range and antiparasitic activities in the low nanomolar range.
Novel azapeptide inhibitors of hepatitis C virus serine protease
Bailey, Murray D.,Halmos, Ted,Goudreau, Nathalie,Lescop, Ewen,Llinàs-Brunet, Montse
, p. 3788 - 3799 (2007/10/03)
Azapeptides are known inhibitors of several serine and cysteine proteases. In seeking different classes of inhibitors for the HCV serine protease, a series of novel azapeptide-based inhibitors were investigated which incorporated noncleavable P1/P1′ aza-a