Highlights
Potency of peptides target to M
pro
and ACE2 were investigated by molecular docking.
Gly143 and Gln189 played key roles in the interactions of peptide E-M and M
pro
.
The RBD of ACE2 was occupied by peptide E-M to inhibit the activity of SARS-CoV-2.
Peptide E-M may be the potent nutritional supplement for COVID-19 patients.
Acetylcholinesterase (AChE), butyrylcholinesterase (BChE), and beta-secretase 1 (BACE 1) play vital roles in the development and progression of Alzheimer's disease (AD).
Summary
Poor understanding of the absorption of food‐derived angiotensin‐converting enzyme (ACE) inhibitory peptides across the membrane limits their application in regulating and preventing hypertension. This study investigated the interaction of egg‐derived ACE inhibitory tri‐peptides ADF, FGR and MIR with the membrane using molecular dynamic simulation and isothermal titration calorimetry (ITC). The structural variations in peptides during absorption were analysed. The effect of peptides on the properties of membranes was also calculated during simulation. The binding mechanism between peptides and membrane was further characterised using ITC. The results showed that the structures of peptides were stable during simulation. Amino acid residues Arg, Phe and Met contributed to the absorption of peptides across the membrane. Hydrogen bonds, electrostatic interactions and hydrophobic interactions stabilised the interaction of peptides with the membrane. The absorption of peptides ADF, FGR and MIR into the membrane increased the membrane thickness of 0.78, 0.82 and 0.80 nm, respectively, and increased lipid lateral diffusion. The ITC results showed that peptides FGR and MIR binding to the membrane were spontaneous, entropy driven and hydrophobic residues Phe and Met of peptides might contribute to peptides‐membrane interactions, which was consistent with molecular dynamic simulation results.
Bitter taste receptor 14(T2R14) is one of the most widely regulated bitter taste Receptors(T2Rs), and plays a vital role in the research of T2Rs blockers. In this study, potential T2R14...
The aim of the present study was to investigate the effect of peptides derived from Colla corii asini on tyrosinase. The sequences of Colla corii asini-derived peptides were identified using mass spectrometry. To characterise the potential peptides with tyrosinase inhibitory activity and clarify their molecular mechanism, both in silico digestion and molecular docking were used. In addition, the tyrosinase inhibitory activities of potential peptides in vitro were also validated. The results showed that Colla corii asini consisted of 472 peptides, and most peptides derived from collagen. Peptides DGGR, DGD, NAGE, LVGE and GSEG were released from the digestion of Colla corii asini-derived peptides and possessed potent inhibitory activity against tyrosinase with IC 50 values of 0.92, 0.50, 0.77, 0.66 and 0.69 mg mL À1 , respectively. The molecular interaction results showed that hydrogen bond and van der Waals interactions are important forces in the interaction of peptides with tyrosinase. Surface forces containing aromatic interaction, hydrogen bond, hydrophilicity and solvent-accessible surface contributed to the interaction between tyrosinase and peptides.
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