Abstract
HPLC-ESI-MS/MS, molecular docking simulation and in situ single-pass intestinal perfusion (SPIP) study were used to identify, select, and confirm the binding affinities between peptides identified from desalted duck egg white peptides (DPs) and calcium sensing receptor (CaSR), respectively. F3 fraction from DPs possessed superior calcium binding activity (P < 0.05), and 16 peptides enriched aromatic amino acids and other 33 peptides were identified. FAE, FNE, INSW, FDPE and NFE presented well binding affinities with CaSR in molecular docking. Additionally, SPIP results showed that NFE and INSW significantly reduced the increased PTH levels by 45.8% and 48.8%, respectively (P < 0.05), and increased calcium percent absorption, calcium absorption rate constant (Ka) and calcium effective permeability (Peff) (P < 0.05), as well as up-regulated mRNA levels of CaSR (P < 0.05). Moreover, NFE and INSW could interact with the VFT domain of CaSR, which exhibited the potential activities in regulation of CaSR.
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