Date published: 2025-9-11

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BC027344 Activators

SIRT1 Activators consist of a variety of chemical compounds that enhance the functional activity of SIRT1 through different mechanisms. Resveratrol, a well-known activator, binds directly to the N-terminal domain of SIRT1, causing a conformational change that amplifies its deacetylase function. Synthetic activators like SRT1720 and SRT2104 operate similarly by engaging with the SIRT1 enzyme to augment its activity. Additionally, natural flavonoids and polyphenols such as Quercetin and Piceatannol modulate upstream pathways, like the AMPK pathway in the case of Quercetin, which indirectly enhance SIRT1 activity by increasing levels of NAD+, a crucial co-substrate for SIRT1's enzymatic action. Fisetin and Isoliquiritigenin also contribute to this activation by influencing signaling pathways that affect NAD+ biosynthesis and the cellular redox state, crucial factors for optimal SIRT1 function.

Continuing with the theme of indirect activators, compounds such as Oleuropein and Cyanidin-3-O-glucoside may activate SIRT1 by elevating NAD+ levels or through antioxidant properties that impact the enzyme's activity. Meanwhile, SRT1460, SRT2183, and SRT3025 are specifically designed to bind SIRT1, leading to increased deacetylation of target proteins, thereby enhancing the regulatory roles played by SIRT1 in cellular processes such as metabolism, DNA repair, and aging.

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