Development of Selective ADAMTS-5 Peptide Substrates to Monitor Proteinase Activity.
Journal
Journal of medicinal chemistry
ISSN: 1520-4804
Titre abrégé: J Med Chem
Pays: United States
ID NLM: 9716531
Informations de publication
Date de publication:
09 03 2023
09 03 2023
Historique:
entrez:
9
3
2023
pubmed:
10
3
2023
medline:
11
3
2023
Statut:
ppublish
Résumé
The dysregulation of proteinase activity is a hallmark of osteoarthritis (OA), a disease characterized by progressive degradation of articular cartilage by catabolic proteinases such as a disintegrin and metalloproteinase with thrombospondin type I motifs-5 (ADAMTS-5). The ability to detect such activity sensitively would aid disease diagnosis and the evaluation of targeted therapies. Förster resonance energy transfer (FRET) peptide substrates can detect and monitor disease-related proteinase activity. To date, FRET probes for detecting ADAMTS-5 activity are nonselective and relatively insensitive. We describe the development of rapidly cleaved and highly selective ADAMTS-5 FRET peptide substrates through
Identifiants
pubmed: 36891740
doi: 10.1021/acs.jmedchem.2c02090
pmc: PMC10009750
doi:
Substances chimiques
Peptides
0
Endopeptidases
EC 3.4.-
ADAMTS4 Protein
EC 3.4.24.82
ADAMTS5 Protein
EC 3.4.24.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
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