Introduction:

Protein Kinase Activated by AMP (AMPK), is a monitor enzyme and a central regulator of the energetic cellular state, therefore, it is responsible for the cellular response to the supply and demand of energy. AMP acts as an activator in conditions of energy deficit, while ATP inactivates it when energy conditions are more favorable. Due to its central role in metabolism, AMPK appears as a promising protein target for the treatment of different diseases such as Diabetes Mellitus type 2 (DM2), Metabolic Syndrome (SM), and Cancer among others. There are multiple isoforms of AMPK that are regulated and differentially expressed throughout the body. The β2-AMPK isoform is expressed almost exclusively in skeletal muscle and since this is the primary organ for Glucose disposal and storage, β2-AMPK has an established role as a driver of insulin-independent Glucose clearance. The activator SC4 has a high selectivity for β2-AMPK and due to its biological function; it could serve as a pharmacological model to aid the treatment of metabolic diseases.

Objective:

To analize the molecular dinamic of AMPK- β2 activation.

Methodology:

In the present work we employed bioinformatics, Chimera 1.15 and Phyton Molecular Viewer.

Results:

The in silico analysis allow us to understand many many structural features related to the action of SC4 on the trimeric structure of AMPK, the specific amino acids involved in the interaction and how its chemical structure gives it high selectivity. Thus, this structural analysis will be useful in order to broaden the criteria for extraction, identification and/or design of active compounds from natural sources, with similar or even better properties than SC4, to use them in a future, with a therapeutic approach that benefits our population.

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