A New Affinity-Based Probe to Profile MMP Active Forms.
Affinity-based probes
Mass spectrometry
Matrix metalloproteinases
Streptavidin-based enrichment
Journal
Methods in molecular biology (Clifton, N.J.)
ISSN: 1940-6029
Titre abrégé: Methods Mol Biol
Pays: United States
ID NLM: 9214969
Informations de publication
Date de publication:
2024
2024
Historique:
medline:
4
12
2023
pubmed:
1
12
2023
entrez:
1
12
2023
Statut:
ppublish
Résumé
A new generation of affinity-based probes (AfBPs) has been developed to label and identity matrix metalloproteinases (MMPs) under their active form in complex proteomes. First, the probe reacts with an active MMP through a proximity-driven reaction that does not require any external trigger. Following this affinity-labeling step, a streptavidin-based enrichment of the resulting biotin-tagged MMP is carried out. Finally, after on-beads proteolytic digestion by trypsin, MMP signature peptides are analyzed and identified by mass spectrometry. Such a "photoactivation-free" labeling can be applied to the detection of several MMPs in a wide variety of biological systems, including in vivo conditions.
Identifiants
pubmed: 38038929
doi: 10.1007/978-1-0716-3589-6_3
doi:
Substances chimiques
Matrix Metalloproteinases
EC 3.4.24.-
Streptavidin
9013-20-1
Biotin
6SO6U10H04
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
29-39Informations de copyright
© 2024. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.
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