Design and synthesis of renin inhibitors: Incorporation of transition- state isostere side chains that span from the S1 to the S3 binding pockets and examination of P3-modified renin inhibitors

Article abstract of DOI:10.1021/jm00015a012

A series of renin inhibitors were designed to examine the topography of the contiguous binding pocket of renin that is normally occupied by the P1 and P3 side chains. Molecular modeling suggested that extending the P1 hydrophobic side chain into the adjac