2va5

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File:2va5.jpg


2va5, resolution 2.75Å

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X-RAY CRYSTAL STRUCTURE OF BETA SECRETASE COMPLEXED WITH COMPOUND 8C

OverviewOverview

Fragment-based lead generation has led to the discovery of a novel series, of cyclic amidine-based inhibitors of beta-secretase (BACE-1). Initial, fragment hits with an isocytosine core having millimolar potency were, identified via NMR affinity screening. Structure-guided evolution of these, fragments using X-ray crystallography together with potency determination, using surface plasmon resonance and functional enzyme inhibition assays, afforded micromolar inhibitors. Similarity searching around the, isocytosine core led to the identification of a related series of, inhibitors, the dihydroisocytosines. By leveraging the knowledge of the, ligand-BACE-1 recognition features generated from the isocytosines, the, dihydroisocytosines were efficiently optimized to submicromolar potency., Compound 29, with an IC50 of 80 nM, a ligand efficiency of 0.37, and, cellular activity of 470 nM, emerged as the lead structure for future, optimization.

About this StructureAbout this Structure

2VA5 is a Single protein structure of sequence from Homo sapiens with and as ligands. Active as Memapsin 2, with EC number 3.4.23.46 Known structural/functional Sites: and . Full crystallographic information is available from OCA.

ReferenceReference

Application of Fragment-Based Lead Generation to the Discovery of Novel, Cyclic Amidine beta-Secretase Inhibitors with Nanomolar Potency, Cellular Activity, and High Ligand Efficiency., Edwards PD, Albert JS, Sylvester M, Aharony D, Andisik D, Callaghan O, Campbell JB, Carr RA, Chessari G, Congreve M, Frederickson M, Folmer RH, Geschwindner S, Koether G, Kolmodin K, Krumrine J, Mauger RC, Murray CW, Olsson LL, Patel S, Spear N, Tian G, J Med Chem. 2007 Nov 29;50(24):5912-5925. Epub 2007 Nov 7. PMID:17985862

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