198208-01-4Relevant academic research and scientific papers
Impact of stereochemistry on ligand binding: X-ray crystallographic analysis of an epoxide-based HIV protease inhibitor
Benedetti, Fabio,Berti, Federico,Campaner, Pietro,Fanfoni, Lidia,Demitri, Nicola,Olajuyigbe, Folasade M.,De March, Matteo,Geremia, Silvano
supporting information, p. 968 - 972 (2014/12/10)
A new pseudopeptide epoxide inhibitor, designed for irreversible binding to HIV protease (HIV-PR), has been synthesized and characterized in solution and in the solid state. However, the crystal structure of the complex obtained by inhibitor-enzyme cocrys
A general and highly selective chelate-controlled intermolecular oxidative heck reaction
Delcamp, Jared H.,Brucks, Alexandria P.,White, M. Christina
supporting information; experimental part, p. 11270 - 11271 (2009/02/05)
A novel chelate-controlled intermolecular oxidative Heck reaction is reported that proceeds with a wide range of nonresonance stabilized α-olefin substrates and organoboron reagents to afford internal olefin products in good yields and outstanding regio- and E:Z stereoselectivities. Pd-H isomerization, common in many Heck reactions, is not observed under these mild, oxidative conditions. This is evidenced by outstanding E:Z selectivities (>20:1 in all cases examined), no erosion in optical purity for proximal stereogenic centers, and a tolerance for unprotected alcohols. Remarkably, a single metal/ligand combination, Pd/bis-sulfoxide complex 1, catalyzes this reaction over a broad range of coupling partners. Given the high selectivities and broad scope, we anticipate this intermolecular Heck reaction will find heightened use in complex molecule synthesis. Copyright
Small hydroxyethylene-based peptidomimetics inhibiting both HIV-1 and C. albicans aspartic proteases
Tossi, Alessandro,Benedetti, Fabio,Norbedo, Stefano,Skrbec, Damiano,Berti, Federico,Romeo, Domenico
, p. 4719 - 4727 (2007/10/03)
We have extended a highly flexible method for rapidly assembling aspartic protease inhibitors to produce symmetric and asymmetric monohydroxyethylene peptidomimetics. This method is based on the prior synthesis of the central non-cleavable peptide-bond is
