Design and Synthesis of Conformationally Restricted Renin Inhibitors,
Abstract
Constrained cyclic peptides have shown to be useful probes in the exploration of the conformational features of the peptide necessary for binding. In designing conformationally restricted analogs of peptides that exist in the extended conformation and contain two hydrophobic side chains on the same side, a constraint that covalently links these side chains with a hydrophobic spacer offers the advantage of maintaining hydrogen bonds between the backbone of the inhibitor and the enzyme while maximizing the hydrophobic interactions of the side chains and the binding properties of the individual side chains.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jan 01, 1992
- Accession Number
- ADP008547
Entities
People
- C. E. Brotherton-pleiss
- L. D. Waterbury
- M. S. Schwartzberg
- S. R. Newman