Identification of potent inhibitors of the sortilin-progranulin interaction.
Bioorg Med Chem Lett
; 30(17): 127403, 2020 09 01.
Article
in En
| MEDLINE
| ID: mdl-32738972
ABSTRACT
High-throughput screening methods have been used to identify two novel series of inhibitors that disrupt progranulin binding to sortilin. Exploration of structure-activity relationships (SAR) resulted in compounds with sufficient potency and physicochemical properties to enable co-crystallization with sortilin. These co-crystal structures supported observed SAR trends and provided guidance for additional avenues for designing compounds with additional interactions within the binding site.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Adaptor Proteins, Vesicular Transport
/
Small Molecule Libraries
/
Progranulins
Type of study:
Diagnostic_studies
/
Prognostic_studies
Limits:
Humans
Language:
En
Journal:
Bioorg Med Chem Lett
Journal subject:
BIOQUIMICA
/
QUIMICA
Year:
2020
Type:
Article