Charting the ligandable proteome for stereoselective interactions

Charting the ligandable proteome for stereoselective interactions

Determining the ligandability of the human proteome can provide key insights to characterize biological processes and promote drug discovery. Now, multi-tiered activity-based protein profiling provides comprehensive proteomic maps of chiral small-molecule interactions. Over 300 distinctive proteins...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Nature chemistry 2024-10, Vol.16 (10), p.1571-1573
Hauptverfasser: Pezacki, John Paul, Lundrigan, Eryn, Evers, Parrish, Uguccioni, Spencer
Format: Artikel
Sprache:eng
Schlagworte:
631/92/475
639/638/309
Analytical Chemistry
Binding sites
Biochemistry
Biological activity
Cell division
Chemistry
Chemistry and Materials Science
Chemistry/Food Science
Inorganic Chemistry
Libraries
Ligands
Mapping
Metabolism
Metabolites
News & Views
news-and-views
Organic Chemistry
Peptides
Physical Chemistry
Proteins
Proteomes
Proteomics
Stereoselectivity
Tryptoline
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
Beschreibung
Zusammenfassung:Determining the ligandability of the human proteome can provide key insights to characterize biological processes and promote drug discovery. Now, multi-tiered activity-based protein profiling provides comprehensive proteomic maps of chiral small-molecule interactions. Over 300 distinctive proteins were identified to ligand tryptoline acrylamides, including stereoselective and site-specific events.
ISSN:1755-4330
1755-4349
1755-4349
DOI:10.1038/s41557-024-01639-1