Structure-based design of highly selective β-secretase inhibitors: synthesis, biological evaluation, and protein-ligand X-ray crystal structure.

@article{Ghosh2012StructurebasedDO,
  title={Structure-based design of highly selective β-secretase inhibitors: synthesis, biological evaluation, and protein-ligand X-ray crystal structure.},
  author={Arun K. Ghosh and Kalapala Venkateswara Rao and Navnath Dnyanoba Yadav and David Deloyd Anderson and Navnath Gavande and Xiangping Huang and Simon S Terzyan and Jordan Jien-nan. Tang},
  journal={Journal of medicinal chemistry},
  year={2012},
  volume={55 21},
  pages={
          9195-207
        }
}
The structure-based design, synthesis, and X-ray structure of protein-ligand complexes of exceptionally potent and selective β-secretase inhibitors are described. The inhibitors are designed specifically to interact with S(1)' active site residues to provide selectivity over memapsin 1 and cathepsin D. Inhibitor 5 has exhibited exceedingly potent inhibitory activity (K(i) = 17 pM) and high selectivity over BACE 2 (>7000-fold) and cathepsin D (>250000-fold). A protein-ligand crystal structure… CONTINUE READING
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