Design and synthesis of unsymmetrical peptidyl urea inhibitors of aspartic peptidases
| Autor: | Daniel H. Rich, Regine S. Bohacek, Natalie A. Dales, Kenneth A. Satyshur |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
Stereochemistry
Protein Conformation Swine Crystal structure Crystallography X-Ray Biochemistry chemistry.chemical_compound Structure-Activity Relationship Pepsin Aspartic Peptidase Animals Aspartic Acid Endopeptidases Urea Computer Simulation Protease Inhibitors Physical and Theoretical Chemistry biology Organic Chemistry Combinatorial chemistry Pepsin A Enzyme inhibition chemistry Drug Design biology.protein Peptides |
| Zdroj: | Organic letters. 3(15) |
| ISSN: | 1523-7060 |
| Popis: | [structure: see text] The design, synthesis, and enzyme inhibition of a new class of aspartic peptidase inhibitors is described. Unsymmetrical ureas were designed from computer-generated structures. Using mechanism-based and substrate-based design techniques, potent pepsin inhibitors were developed and the binding mode was established. Two X-ray crystal structures of enzyme-bound inhibitors revealed a new binding mode that is closely related to the computer-generated binding mode. |
| Databáze: | OpenAIRE |
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