Exploratory experiment designed to discover new patterns targeting ACAT1 in in vitro protein-ligand binding assays. Primary outcome: confirmation of direct hyperoside-ACAT1 binding
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.
cellular thermal shift assays, surface plasmon resonance, molecular docking, ubiquitination assays
hyperoside would directly bind to and stabilize ACAT1
detectable binding affinity and thermal stabilization of ACAT1
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