Tier 3 — preclinical

Ursolic acid activates SIRT6 by enhancing enzyme-substrate interactions and promoting protein structural rearrangement

Zohreh Tabatabaian Nimavard, Nuredin Bakhtiari, Fereshteh Taghavi, Sako Mirzaie, Farangis Ataei, Hamid-Reza Khaledi
Biochimica et Biophysica Acta (BBA) - General Subjects 2026 1870(2):130890

Bibliography

PubMed
PMID 41314263

Study snapshot

DesignMolecular-dynamics simulation plus purified recombinant SIRT6 enzyme kinetics and spectroscopic structural analysis.
ModelRecombinant human SIRT6 expressed in E. coli; in-silico SIRT6-ursolic-acid modeling.
SampleBiochemical replicate experiments; not a human or animal intervention cohort.
InterventionUrsolic acid exposure to purified SIRT6.
DurationAcute biochemical assays.
EndpointsSIRT6 binding energy and stability; Km; Vmax; Kcat; Kcat/Km; Protein secondary structure and aggregation index

What the study showed, in plain terms

Ursolic acid directly altered purified SIRT6 in biochemical and computational experiments, increasing catalytic-efficiency measures and stabilizing a more favorable enzyme conformation. The study supports ursolic acid as a new direct SIRT6 activator candidate but does not show that food or supplements activate SIRT6 in people.

Key findings

Ursolic acid lowered the reported Km, increased Vmax and Kcat, improved catalytic efficiency, and induced measurable SIRT6 structural rearrangement in purified-enzyme experiments.

What this study can and cannot tell us

The work uses purified protein and molecular simulation. It does not establish cellular target engagement, oral bioavailability, tissue exposure, safety, aging benefits or clinical efficacy.

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