A simple and effective method based on enzyme-ligand complex for affinity analysis of lipase inhibitor from...

Schisandra chinensis (Turcz.) Baill has various biological activities including anti-obesity. Rapid analysis and screening of active compounds from natural extracts is one of the challenges faced by natural drug research. In order to analyze and screen lipase inhibitor from Schisandra chinensis extract, a method inspired by the specific binding of enzyme to ligand was developed and established. Through optimization of incubation conditions, such as time, temperature, and pH, the potential active compound was locked by comparing the change of the chemical components of the S. chinensis extract before and after incubation with lipase. Subsequently, the target compound was isolated by high-speed counter-current chromatography and was identified as 5-hydroxymethyl-2-furaldehyde. Moreover, in vitro activity determination confirmed that 5-hydroxymethyl-2-furaldehyde with an IC₅₀ value of 284.78 ± 16.45 μg/mL interacted with the lipase through non-competitive inhibition. Furthermore, molecular docking further revealed that 5-hydroxymethyl-2-furaldehyde can be embedded into the active pocket of lipase via multiple hydrogen bonds and other interactions. This study not only screened a potential lipase inhibitor from S. chinensis through the newly developed method, but also can be used as a typical reference for the discovery of active components from functional foods and natural products.