🧫
Myricanol-ACSL1 direct binding validation using CETSA and molecular docking
active
experiment
Created: 2026-04-10T22:46:31
By: etl-v1-backfill
Quality:
50%
✓ SciDEX
ID: exp-feac9870-b737-4a77-8438-302f8eed1e47
🧫 Experiment Protocol
ExploratoryhyperlipidemiaACSL1, SCD1mouse serum, computational molecular dockingproposed
This molecular interaction study employed cellular thermal shift assay (CETSA), molecular docking, and ELISA to confirm direct binding between myricanol and ACSL1 protein. The CETSA technique was used to demonstrate thermal stabilization of ACSL1 upon myricanol binding, while molecular docking provided computational validation of the binding interaction. ELISA measurements confirmed that myricanol treatment decreased concentrations of both ACSL1 and SCD1 in mouse serum. This experiment provided crucial mechanistic evidence that myricanol directly targets ACSL1 protein, establishing a molecular basis for its lipid-lowering effects through the ACSL1-SCD1 axis. The combination of biophysical, computational, and biochemical approaches provided robust evidence for direct protein-drug interaction.
PRIMARY OUTCOME
direct binding confirmation between myricanol and ACSL1
EXPECTED OUTCOMES
Thermal stabilization of ACSL1 by myricanol, favorable docking scores, decreased serum ACSL1 and SCD1 concentrations
SUCCESS CRITERIA
Positive CETSA results indicating protein stabilization, computationally favorable binding interactions, significant reduction in serum protein levels
PROTOCOL
Cellular thermal shift assay (CETSA) for protein thermal stabilization, molecular docking analysis for binding prediction, ELISA for serum protein concentration measurement
Source: PMID 41520958 ↗
🧫 Experiment Extras
PATHWAY
ACSL1-SCD1 axis, fatty acid metabolism
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.