کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1374909 | 981927 | 2009 | 5 صفحه PDF | دانلود رایگان |
A novel series of isatin-based inhibitors of β-secretase (BACE-1) have been identified using a virtual high-throughput screening approach. Structure–activity relationship studies revealed structural features important for inhibition. Docking studies suggest these inhibitors may bind within the BACE-1 active site through H-bonding interactions involving the catalytic aspartate residues.
A novel series of isatin-based inhibitors of β-secretase (BACE-1) have been identified using a virtual high-throughput screening approach. Structure–activity relationship studies revealed structural features important for inhibition. Docking studies suggest these inhibitors may bind within the BACE-1 active site through H-bonding interactions involving the catalytic aspartate residues.Figure optionsDownload as PowerPoint slide
Journal: Bioorganic & Medicinal Chemistry Letters - Volume 19, Issue 23, 1 December 2009, Pages 6770–6774