Pancreatic Lipase Inhibition Strategies for Obesity Management

Pancreatic lipase is the principal enzyme responsible for hydrolysing dietary triglycerides into absorbable free fatty acids and monoacylglycerols. Inhibition of this enzyme reduces fat absorption and represents a validated approach to weight control and metabolic health. Traditional pharmacotherapy in this area has centred on orlistat, a covalent inhibitor of pancreatic lipase that reduces lipid uptake but can cause gastrointestinal side effects. Recent efforts have broadened to include non-covalent small molecules, plant-derived polyphenols and peptide-based agents with improved specificity and tolerability. Advances in screening technologies, including microfluidic platforms, and in silico modelling have accelerated the discovery of novel scaffolds and optimisation of binding affinity to the lipase active site. Parallel research explores formulation approaches to enhance the bioavailability of natural inhibitors and to mitigate adverse effects. Collectively, these strategies aim to deliver efficacious, safe and patient-friendly interventions that complement lifestyle measures in the global management of obesity.

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Pancreatic Lipase Inhibition Strategies for Obesity Management publication trend

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Technical terms

Pancreatic lipase: A digestive serine hydrolase that catalyses the hydrolysis of dietary triglycerides in the small intestine.

IC50: The concentration of an inhibitor required to reduce enzyme activity by 50%, a standard measure of potency.

Non-competitive inhibition: A mode of enzyme inhibition in which the inhibitor binds to an allosteric site distinct from the active site, reducing catalytic activity irreversibly or reversibly.

Molecular docking: A computational method for predicting the preferred orientation and binding affinity of a small molecule ligand within a target protein’s active site.

References

1. Construction and Manipulation of Serial Gradient Dilution Array on a Microfluidic Slipchip for Screening and Characterizing Inhibitors against Human Pancreatic Lipase. Biosensors (2023).
2. Exploring Aurone Derivatives as Potential Human Pancreatic Lipase Inhibitors through Molecular Docking and Molecular Dynamics Simulations. Molecules (2020).
3. Polyphenolic Compounds and Digestive Enzymes: In Vitro Non-Covalent Interactions. Molecules (2017).