Preparation and Characterization of a Sea Cucumber Collagen-Derived Peptide and the Inhibition of Pancreatic Lipase

The effective modulation of pancreatic lipase activities is critical in maintaining blood triglycerides and cholesterol levels within normal physiological ranges. This study investigated the inhibitory effect of peptides from sea cucumber collagen on pancreatic lipase activity through interaction with the Ca-binding sites on the enzyme. Among the five sea cucumber collagen digests (SCCD), the pepsin-digested 2h+trypsin-digested 3h digest (SDP2h+T3h) showed the strongest inhibitory effect on pancreatic lipase. A peptide RDDPEPSYK (RDD), with a sequence of Arg-Asp-Asp-Pro-Glu-Pro-Ser-Tyr-Lys from SDP2h+T3h, was found to target the Ca-binding site of pancreatic lipase, interacting with certain residues including Asp184, Glu187, Lys163, etc. Additionally, a cell study on 3T3-L1 preadipocytes indicated RDD's capability to inhibit adipocyte differentiation, as well as decrease intracellular triglycerides, total cholesterol, and lipid content. The results from this study suggest that RDD is a targeted pancreatic lipase inhibitor with potential applications for obesity control.