Design and synthesis of diaminopyrrolidinone inhibitors of human osteoclast cathepsin K

The structure-based design and synthesis of lactam-constrained azapeptide inhibitors of human cathepsin K are described. Enhanced stability to proteolytic cleavage over acyclic analogues is discussed. The structure-based design and synthesis of lactam-constrained azapeptide inhibitors (e.g., 2) of h...

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Bibliographic Details
Published in:Bioorganic & medicinal chemistry letters 1999-07, Vol.9 (14), p.1907-1910
Main Authors: Duffy, Kevin J., Ridgers, Lance H., DesJarlais, Renee L., Tomaszek, Thaddeus A., Bossard, Mary J., Thompson, Scott K., Keenan, Richard M., Veber, Daniel F.
Format: Article
Language:English
Subjects:
Amines - chemistry
Biological and medical sciences
Bones, joints and connective tissue. Antiinflammatory agents
Cathepsin K
Cathepsins - antagonists & inhibitors
Cathepsins - metabolism
Crystallography, X-Ray
Cysteine Proteinase Inhibitors - chemical synthesis
Cysteine Proteinase Inhibitors - metabolism
Cysteine Proteinase Inhibitors - pharmacology
Drug Design
Humans
Medical sciences
Models, Molecular
Osteoclasts - enzymology
Peptides - chemistry
Pharmacology. Drug treatments
Pyrrolidinones - chemical synthesis
Pyrrolidinones - metabolism
Pyrrolidinones - pharmacology
Structure-Activity Relationship
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Summary:The structure-based design and synthesis of lactam-constrained azapeptide inhibitors of human cathepsin K are described. Enhanced stability to proteolytic cleavage over acyclic analogues is discussed. The structure-based design and synthesis of lactam-constrained azapeptide inhibitors (e.g., 2) of human osteoclast cathepsin K are described.
ISSN:0960-894X
1464-3405
DOI:10.1016/S0960-894X(99)00322-4