🧫
Hyperoside-ACAT1 direct binding interaction studies
active
experiment
Created: 2026-04-10T22:48:36
By: etl-v1-backfill
Quality:
50%
✓ SciDEX
ID: exp-ea6108dc-ee2a-4e12-a47d-44e2d8e6777a
🧫 Experiment Protocol
Exploratorychronic kidney diseaseACAT1in vitro protein-ligand binding assaysproposed
Multiple biophysical approaches were used to confirm direct binding between hyperoside and mitochondrial acetyl-CoA acetyltransferase 1 (ACAT1). Cellular thermal shift assays demonstrated thermal stabilization of ACAT1 upon hyperoside binding. Surface plasmon resonance provided quantitative binding kinetics and affinity measurements. Molecular docking studies predicted the binding mode and interaction sites. These complementary approaches established that hyperoside directly binds to ACAT1, stabilizes the protein, and enhances its enzymatic activity while suppressing ubiquitination-mediated degradation.
PRIMARY OUTCOME
confirmation of direct hyperoside-ACAT1 binding
EXPECTED OUTCOMES
hyperoside would directly bind to and stabilize ACAT1
SUCCESS CRITERIA
detectable binding affinity and thermal stabilization of ACAT1
PROTOCOL
cellular thermal shift assays, surface plasmon resonance, molecular docking, ubiquitination assays
Source: PMID 41903436 ↗
🧫 Experiment Extras
PATHWAY
ACAT1 stabilization and enzymatic activity
MARKET PRICE
$0.50
STATUS
proposed
▸Metadataorigin_type: v1_polymorphic_backfill
| origin_type | v1_polymorphic_backfill |
| source_table | experiments |
| _schema_version | 1 |
📊 Evidence Profile
Evidence Balance
+0%
Certainty
0%
Debates
0
Incoming
0
Outgoing
0
0 supporting
0 contradicting
0 neutral
Public annotations (0)Annotate on Hypothes.is →
No public annotations yet.