BACKGROUND
Egg derived peptides were becoming more and more popular due to their good biological activity and non-toxic side effects. The egg derived peptides Arg-Val-Pro-Ser-Leu (RVPSL) and Gln-Ile-Gly-Leu-Phe (QIGLF) possessed high angiotensin-converting enzyme inhibitory activity and it could be taken up by intestinal epithelial cells. The interaction of egg derived peptides RVPSL and QIGLF with the membrane remains unclear.
RESULTS
The position and structure of the peptide in the membrane were calculated. Maximum density values of peptides RVPSL and QIGLF were 2. 27 nm and 1. 22 nm away from the center of 1,2-dipalmitoyl-sn-glycero-3-phosphatidylcholine (DPPC) membrane, indicating that peptides penetrated the membrane-water interface and were embedded in the membrane. The interaction of RVPSL and QIGLF with the DPPC membrane did not affect the average area per lipid and lipid sequence parameters. The thermodynamic parameters ΔH, ΔG and ΔS of the interaction between peptide RVPSL with DPPC membrane were 17. 91 kJ·mol-1 , -17. 63 kJ·mol-1 , 187. 5 J·mol-1 ·k-1 , respectively. The thermodynamic parameters ΔH, ΔG and ΔS of the interaction between peptide QIGLF with DPPC membrane were 17. 10 kJ·mol-1 , -17. 12 kJ·mol-1 , 114. 8 J·mol-1 ·k-1 , respectively.
CONCLUSION
The indicated that the binding of peptides RVPSL and QIGLF to DPPC was an endothermic, spontaneous and entropy-driven reaction. The results of the study provided reference and guidanced for solving the problem of the low bioavailability of bioactive peptides (BP). This article is protected by copyright. All rights reserved.