Design and synthesis of a new class of conformationally constrained inhibitors to probe the active sites of thermolysine and neutral endopeptidase 24.11

Article abstract of DOI:10.1016/0960-894X(96)00375-7

The design as well as the synthesis, resolution, and biological evaluation of the neutral endopeptidase 24.11 inhibitors, (1S,2R,5S)-(-)-[(2-mercapto-5-phenyl-cyclopentanecarbonyl)-amino]-acet ic acid and (1R,2S,5R)-(+)-[(2-mercapto-5-phenyl-cyclopentanecarbonyl)-amino]-acet ic acid are described.