Abstract：
BACKGROUND: Egg-derived peptides are becoming increasingly popular due to their biological activity and non-toxic effects. The egg-derived peptides Arg-Val-Pro-Ser-Leu (RVPSL) and Gln-Ile-Gly-Leu-Phe (QIGLF) display strong angiotensin-converting enzyme inhibitory activity and they can be taken up by intestinal epithelial cells. The interaction of the egg-derived peptides RVPSL and QIGLF with the membrane remains unclear.
RESULTS: The position and structure of the peptides in the membrane were calculated. The maximum density values of RVPSL and QIGLF were 2.27 and 1.22 nm from the center of the 1,2-dipalmitoyl-sn-glycero-3-phosphatidylcholine (DPPC) membrane, respectively, 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 or the lipid sequence parameters. The thermodynamic parameters ΔH, ΔG, and ΔS of the interaction between the peptide RVPSL with the 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.
CONCLUSIONS: The results indicated that the binding of peptides RVPSL and QIGLF to DPPC is an endothermic, spontaneous, and entropy-driven reaction. The results of the study are relevant to the problem of the low bioavailability of bioactive peptides (BP). © 2023 Society of Chemical Industry.
RESULTS: The position and structure of the peptides in the membrane were calculated. The maximum density values of RVPSL and QIGLF were 2.27 and 1.22 nm from the center of the 1,2-dipalmitoyl-sn-glycero-3-phosphatidylcholine (DPPC) membrane, respectively, 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 or the lipid sequence parameters. The thermodynamic parameters ΔH, ΔG, and ΔS of the interaction between the peptide RVPSL with the 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.
CONCLUSIONS: The results indicated that the binding of peptides RVPSL and QIGLF to DPPC is an endothermic, spontaneous, and entropy-driven reaction. The results of the study are relevant to the problem of the low bioavailability of bioactive peptides (BP). © 2023 Society of Chemical Industry.
摘要：
背景：鸡蛋衍生肽由于其良好的生物活性和无毒副作用而变得越来越受欢迎。卵衍生肽Arg-Val-Pro-Ser-Leu（RVPSL）和Gln-Ile-Gly-Leu-Phe（QIGLF）具有较高的血管紧张素转换酶抑制活性，可被肠上皮细胞吸收。卵源肽RVPSL和QIGLF与膜的相互作用尚不清楚。
结果：计算了肽在膜中的位置和结构。肽RVPSL和QIGLF的最年夜密度值分离为2。27nm和1。距离1,2-二棕榈酰-sn-甘油-3-磷脂酰胆碱（DPPC）膜中心22nm，表明肽穿透膜-水界面并嵌入膜中。RVPSL和QIGLF与DPPC膜的相互作用不影响每个脂质的平均面积和脂质序列参数。热力学参数ΔH，肽RVPSL与DPPC膜之间相互作用的ΔG和ΔS分别为17。91kJ·mol-1,-17.63kJ·mol-1,187.5J·mol-1·k-1，分别。热力学参数ΔH，肽QIGLF与DPPC膜之间相互作用的ΔG和ΔS分别为17。10kJ·mol-1,-17.12kJ·mol-1,114.8J·mol-1·k-1，分别。
结论：表明肽RVPSL和QIGLF与DPPC的结合是吸热的，自发和熵驱动的反应。研究结果为解决生物活性肽生物利用度低的问题提供了参考和指导。本文受版权保护。保留所有权利。
结果：计算了肽在膜中的位置和结构。肽RVPSL和QIGLF的最年夜密度值分离为2。27nm和1。距离1,2-二棕榈酰-sn-甘油-3-磷脂酰胆碱（DPPC）膜中心22nm，表明肽穿透膜-水界面并嵌入膜中。RVPSL和QIGLF与DPPC膜的相互作用不影响每个脂质的平均面积和脂质序列参数。热力学参数ΔH，肽RVPSL与DPPC膜之间相互作用的ΔG和ΔS分别为17。91kJ·mol-1,-17.63kJ·mol-1,187.5J·mol-1·k-1，分别。热力学参数ΔH，肽QIGLF与DPPC膜之间相互作用的ΔG和ΔS分别为17。10kJ·mol-1,-17.12kJ·mol-1,114.8J·mol-1·k-1，分别。
结论：表明肽RVPSL和QIGLF与DPPC的结合是吸热的，自发和熵驱动的反应。研究结果为解决生物活性肽生物利用度低的问题提供了参考和指导。本文受版权保护。保留所有权利。
