Back to Search
Start Over
Calpain inhibitors based on the quiescent affinity label concept: high rates of calpain inactivation with leaving groups derived from N-hydroxy peptide coupling reagents
- Source :
- Bioorganic & Medicinal Chemistry Letters. 10:2315-2319
- Publication Year :
- 2000
- Publisher :
- Elsevier BV, 2000.
-
Abstract
- A series of irreversible inhibitors of recombinant calpain has been synthesized and their rates of inactivation have been evaluated against calpain and cathepsin B, respectively. The design of the inhibitors was based on the quiescent affinity label concept. By choosing the appropriate affinity group and by employing leaving groups derived from N-hydroxy coupling reagents, good inhibitors of calpain with high rates of inactivation have been identified. However, poor aqueous stability limits their therapeutic utility.
- Subjects :
- Affinity label
Clinical Biochemistry
Pharmaceutical Science
Peptide
Cysteine Proteinase Inhibitors
Biochemistry
Cathepsin B
law.invention
Structure-Activity Relationship
law
Drug Discovery
Humans
Structure–activity relationship
Molecular Biology
chemistry.chemical_classification
biology
Calpain
Organic Chemistry
Affinity Labels
Dipeptides
Recombinant Proteins
Enzyme
chemistry
Enzyme inhibitor
Drug Design
biology.protein
Recombinant DNA
Molecular Medicine
Indicators and Reagents
Oligopeptides
Subjects
Details
- ISSN :
- 0960894X
- Volume :
- 10
- Database :
- OpenAIRE
- Journal :
- Bioorganic & Medicinal Chemistry Letters
- Accession number :
- edsair.doi.dedup.....b51e852c2d7642f9ca18c7c2397a6766