Identification of a Small Molecule Nonpeptide Active Site β-Secretase Inhibitor That Displays a Nontraditional Binding Mode for Aspartyl Proteases

Abstract
A small molecule nonpeptide inhibitor of β-secretase has been developed, and its binding has been defined through crystallographic determination of the enzyme−inhibitor complex. The molecule is shown to bind to the catalytic aspartate residues in an unprecedented manner in the field of aspartyl protease inhibition. Additionally, the complex reveals a heretofore unknown S3 subpocket that is created by the inhibitor. This structure has served an important role in the design of newer β-secretase inhibitors.