359781-82-1Relevant academic research and scientific papers
Lysine derivatives as potent HIV protease inhibitors. Discovery, synthesis and structure-activity relationship studies
Bouzide, Abderrahim,Sauve, Gilles,Yelle, Jocelyn
, p. 1509 - 1513 (2007/10/03)
A screening assay program on HIV-protease was carried out on more than fifty commercially available N-protected amino acids and has revealed that those with a long side chain such as lysine, ornithine and arginine exhibited significant inhibition of HIV protease enzyme. The presence of an Fmoc group was found to be essential to obtain micromolar inhibitors and the addition of an alkyl group at the Nα-position resulted in the discovery of the lead compound 11 displaying a 5 nM inhibition constant. Although this new inhibitor series is not categorized among those mimicking the substrate with a non-hydrolyzable transition-state isoster, it was found very specific to inhibit HIV protease enzyme in comparison to the mammalian aspartyl proteases pepsin, renin and cathepsin. Furthermore, these inhibitors did not show any cytotoxicity at a concentration below 75 μM.
Lysine sulfonamides as novel HIV-Protease inhibitors: Optimization of the Nε-acyl-phenyl spacer
Stranix, Brent R.,Sauve, Gilles,Bouzide, Abderrahim,Cote, Alexandre,Sevigny, Guy,Yelle, Jocelyn
, p. 4289 - 4292 (2007/10/03)
A series of Nα-isobutyl-Nα-arylsulfonamido-(Nε acyl) lysine and lysinol derivatives were prepared and evaluated as inhibitors of HIV protease and wild type virus. A simple original synthesis was devised to form Nα-(arylsulfonamide)-Nα-isobutyl lysine, whi
Amino acid derivatives as HIV aspartyl protease inhibitors
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, (2008/06/13)
The present invention relates to a class of amino acid derivatives with HIV aspartyl protease inhibitory properties.
