🧫
Direct targeting of Capza1 by silibinin
active
experiment
Created: 2026-04-11T00:47:39
By: etl-v1-backfill
Quality:
50%
✓ SciDEX
ID: exp-62a384e1-df5f-4345-a072-4183799872ce
🧫 Experiment Protocol
Exploratorybreast cancerCAPZA1, YAP1MCF-7 and MDA-MB-231 human breast cancer cell linesproposed
This experiment focused on identifying the direct molecular target of silibinin that mediates F-actin disassembly. The researchers used biochemical approaches to investigate the interaction between silibinin and F-actin regulatory proteins. They discovered that silibinin directly targets Capza1 (capping actin protein of muscle Z-line subunit alpha 1), which is responsible for F-actin disassembly. The study likely employed techniques such as CETSA (cellular thermal shift assay) and DARTS (drug affinity responsive target stability) to demonstrate direct drug-protein interactions. The researchers showed that Capza1-mediated F-actin disassembly is the decisive mechanism for silibinin-induced cell cycle arrest, even when YAP activity is modulated. This experiment revealed a positive feedback loop between YAP and F-actin, where promoting F-actin assembly through si-Capza1 transfection can restore YAP activity.
PRIMARY OUTCOME
Direct drug-protein interaction and F-actin disassembly
EXPECTED OUTCOMES
Expected to identify direct molecular target of silibinin; found Capza1 as the primary target mediating F-actin disassembly
SUCCESS CRITERIA
Demonstration of direct silibinin-Capza1 interaction and rescue of phenotype by Capza1 knockdown
PROTOCOL
CETSA, DARTS, protein-drug interaction assays, siRNA transfection, F-actin visualization, YAP activity assessment
Source: PMID 41349910 ↗
🧫 Experiment Extras
PATHWAY
actin cytoskeleton organization, actin capping
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.