ArticleCell biochemistry and biophysics2026
Modulation of SERCA1a by Sesquiterpene Lactones: Insights into Inhibition Mechanisms.
Article in Cell biochemistry and biophysics, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
The sarcoplasmic reticulum Ca²⁺-ATPase (SERCA1a) is a key regulator of intracellular calcium homeostasis and an emerging therapeutic target in cancer, cardiac, and metabolic diseases. Sesquiterpene lactones such as thapsigargin (TG) and trilobolide (TB) inhibit SERCA1a via transmembrane binding, yet systematic comparisons of their inhibitory potency and biophysical mechanisms remain limited. Here, we investigated the inhibitory effects of TG, TB, and two TB derivatives (TB-44, TB-46(2)) using kinetic, thermodynamic, and docking analyses. SERCA1a activity in isolated sarcoplasmic reticulum vesicles was quantified by an NADH-coupled ATPase assay, with Ca²⁺- and ATP-dependence modeled by Michaelis-Menten and Hill fits. All compounds inhibited SERCA1a in a dose-dependent manner, with TB most potent (IC₅₀ = 0.36 µM vs. TG 0.60 µM) and TB-44 the most effective derivative (IC₅₀ = 1.47 µM). Each reduced V
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