کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1366721 | 981600 | 2007 | 5 صفحه PDF | دانلود رایگان |

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.
Peptidic, non-covalent inhibitors of lysosomal cysteine protease cathepsin S were investigated due to low oral bioavailability of initial leads, leading to an improved series of peptidomimetic inhibitors utilizing phenyl succinamides as the P2 residue.Figure optionsDownload as PowerPoint slide
Journal: Bioorganic & Medicinal Chemistry Letters - Volume 17, Issue 10, 15 May 2007, Pages 2899–2903