150609-73-7Relevant academic research and scientific papers
Structure-based design, synthesis, and biological evaluation of irreversible human rhinovirus 3C protease inhibitors. 3. Structure-activity studies of ketomethylene-containing peptidomimetics
Dragovich, Peter S.,Prins, Thomas J.,Zhou, Ru,Fuhrman, Shella A.,Patick, Amy K.,Matthews, David A.,Ford, Clifford E.,Meador III, James W.,Ferre, Rose Ann,Worland, Stephen T.
, p. 1203 - 1212 (2007/10/03)
The structure-based design, chemical synthesis, and biological evaluation of various ketomethylene-containing human rhinovirus (HRV) 3C protease (3CP) inhibitors are described. These compounds are comprised of a peptidomimetic binding determinant and an e
HIV-1 protease inhibitors based on hydroxyethylene dipeptide isosteres: An investigation into the role of the P1' side chain on structure-activity
Young,Payne,Thompson,Gaffin,Lyle,Britcher,Graham,Schultz,Deana,Darke,Zugay,Schleif,Quintero,Emini,Anderson,Huff
, p. 1702 - 1709 (2007/10/02)
A systematic investigation was undertaken to determine the role of the P1' sidechain in a series of hydroxyethylene isostere based inhibitors of HIV-1 protease. Substitution and homologation of the benzyl P1' side chain of the Phe-Phe isostere based pseudo peptides 1 (L-682,679) and 2 (L-685,434) with various heteroalkyl groups leads to a series of extremely potent inhibitors of the enzyme. Several examples of the most potent inhibitors were very effective in an ex vivo cell based viral spread assay using human H9 T- lymphocytes and the IIIb isolate of HIV-1. Compound 19 is 120 times more potent than 1 and 16 times more potent than 2 in inhibiting the spread of infection in this assay.
