Exploring the Novel Pancreatic Lipase-Inhibitory Peptides in Chlorella pyrenoidosa: Preparation, Purification, Identification, and Molecular Docking Article Swipe
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· 2025
· Open Access
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· DOI: https://doi.org/10.3390/foods14183277
· OA: W4414389804
Obesity is a worldwide problem, and lowering pancreatic lipase (PL) activity is an effective strategy to counteract it. In this study, pancreatic lipase-inhibitory (PL-I) peptides were isolated and purified from Chlorella pyrenoidosa protein hydrolysates (CPPHs) using ultrafiltration and Sephadex gel chromatography (Sephadex G-25). A total of 858 peptides were identified by liquid chromatography–tandem mass spectrometry (LC-MS/MS). Four novel PL-I peptides (FLSQPF, VWTPI, IVGPF, and IPYPL) were virtually screened using molecular docking and subsequently synthesized, with VWTPI exhibiting the highest PL inhibition. Moreover, the inhibition of the enzyme by VWTPI was a mixture of competitive and non-competitive inhibition, with an inhibition constant (Ki) of 7.27 mg/mL. Molecular docking showed that VWTPI interacts with the PL active center by hydrogen bonding, hydrophobic contacts, van der Waals forces, and π-π stacking. This study suggests that peptides from Chlorella pyrenoidosa could be used as lipid-lowering agents to prevent and cure obesity.
