Egg White-Derived Peptides QVPLW and LCAY Inhibit the Activity of Angiotensin I-Converting Enzyme in Human Umbilical Vein Endothelial Cells by Suppressing Its Recruitment into Lipid Rafts

As a membrane protein, the activity of angiotensin I-converting enzyme (ACE) can be modulated via regulation of its localization in the cell membrane with food-derived peptides. This study aimed to explore the effect of egg white peptides on the cell membrane localization and activity of ACE in human umbilical vein endothelial cells. ACE activity was found to be related to lipid rafts by using methyl-beta-cyclodextrin (M beta CD). QVPLW and LCAY can inhibit ACE activity by preventing ACE recruitment into lipid rafts, with in situ IC50 values of 238.46 +/- 11.35 mu M and 31.55 +/- 2.64 mu M in the control groups, as well as 45.43 +/- 6.15 mu M and 34.63 +/- 1.59 mu M in the M beta CD groups, respectively. QVPLW and LCAY may alter the cell membrane properties, including the fluidity, potential, and permeability, and eventually promote the transposition of ACE.

Automated summary

Egg white peptides can modulate the activity of ACE by affecting its localization in the cell membrane, potentially altering cell membrane properties and promoting the transposition of ACE.