519025-63-9Relevant academic research and scientific papers
Investigating the selectivity of metalloenzyme inhibitors
Day, Joshua A.,Cohen, Seth M.
, p. 7997 - 8007 (2013)
The inhibitory activity of a broad group of known metalloenzyme inhibitors against a panel of metalloenzymes was evaluated. Clinically approved inhibitors were selected as well as several other reported metalloprotein inhibitors in order to represent a broad range of metal binding groups (MBGs), including hydroxamic acid, carboxylate, hydroxypyridinonate, thiol, and N-hydroxyurea functional groups. A panel of metalloenzymes, including carbonic anhydrase (hCAII), several matrix metalloproteinases (MMPs), angiotensin converting enzyme (ACE), histone deacetylase (HDAC-2), and tyrosinase (TY), was selected based on their clinical importance for a range of pathologies. In addition, each inhibitor was evaluated for its ability to remove Fe3+ from holo-transferrin to gauge the ability of the inhibitors to access Fe 3+ from a primary transport protein. The results show that the metalloenzyme inhibitors are quite selective for their intended targets, suggesting that despite their ability to bind metal ions, metalloprotein inhibitors are not prone to widespread off-target enzyme inhibition activity.
HIV INTEGRASE INHIBITORS
-
Page/Page column 61, (2012/08/27)
Provided herein, inter alia, are novel compounds for the inhibition of HIV integrase. The compounds disclosed herein are useful for methods of treating HIV infection in a subject in need thereof.
Scaffold rearrangement of dihydroxypyrimidine inhibitors of HIV integrase: Docking model revisited
Tang, Jing,Maddali, Kasthuraiah,Pommier, Yves,Sham, Yuk Y.,Wang, Zhengqiang
supporting information; experimental part, p. 3275 - 3279 (2010/08/19)
A series of dihydroxypyrimidine (DHP) derivatives were designed as inhibitors of HIV integrase (IN) based on known homology models. Through chemical synthesis and biochemical assays it was found that the activity profile of these compounds largely deviate
