199005-54-4Relevant academic research and scientific papers
Synthesis, activity and structure-activity relationship of noroviral protease inhibitors
Deng, Lisheng,Muhaxhiri, Zana,Estes, Mary K.,Palzkill, Timothy,Venkataram Prasad,Song, Yongcheng
, p. 1354 - 1359 (2013/10/08)
The protease of norovirus, an important human pathogen, is essential for the viral replication and, therefore, represents a potential drug target. A series of tripeptide-based inhibitors of the protease were designed, synthesized and tested, among which several potent inhibitors were identified with K i values as low as 75 nM. The structure-activity relationships of these inhibitors are discussed.
Tripeptide aldehyde inhibitors of human rhinovirus 3C protease: Design, synthesis, biological evaluation, and cocrystal structure solution of P1 glutamine isosteric replacements
Webber, Stephen E.,Okano, Koji,Little, Thomas L.,Reich, Siegfried H.,Xin, Yue,Fuhrman, Sheila A.,Matthews, David A.,Love, Robert A.,Hendrickson, Thomas F.,Patick, Amy K.,Meador III, James W.,Ferre, Rose Ann,Brown, Edward L.,Ford, Clifford E.,Binford, Susan L.,Worland, Stephen T.
, p. 2786 - 2805 (2007/10/03)
The investigation of tripeptide aldehydes as reversible covalent inhibitors of human rhinovirus (HRV) 3C protease (3CP) is reported. Molecular models based on the apo crystal structure of HRV-14 3CP and other trypsin- like serine proteases were constructe
