155674-36-5Relevant academic research and scientific papers
Synthesis and SAR of succinamide peptidomimetic inhibitors of cathepsin S
Chatterjee, Arnab K.,Liu, Hong,Tully, David C.,Guo, Jianhua,Epple, Robert,Russo, Ross,Williams, Jennifer,Roberts, Michael,Tuntland, Tove,Chang, Jonathan,Gordon, Perry,Hollenbeck, Thomas,Tumanut, Christine,Li, Jun,Harris, Jennifer L.
, p. 2899 - 2903 (2008/12/22)
Peptidic, non-covalent inhibitors of lysosomal cysteine protease cathepsin S (1 and 2) were investigated due to low oral bioavailability, leading to an improved series of peptidomimetic inhibitors. Utilizing phenyl succinamides as the P2 residue increased the oral exposure of this lead series of compounds, while retaining selective inhibition of the cathepsin S isoform. Concurrent investigation of the P1 and P2 subsites resulted in the discovery of several potent and selective inhibitors of cathepsin S with good pharmacokinetic properties due to the elimination of saturated aliphatic P2 residues.
Optically active cyclopropanols by samarium(II) iodide induced intramolecular reductive cyclisation of β-chlorosubstituted amides
Fadel
, p. 531 - 534 (2007/10/02)
Samarium diiodide promotes under mild conditions, intramolecular reductive cyclisation of β-chloro substituted amides, and leads with an excellent diastereomeric excess and high yield to functionalised optically active cyclopropranols.
