Interaction between soybean oleosome-associated proteins and phospholipid bilayer and its influence on environmental stability of luteolin-loaded liposomes

Abstract

Soybean oleosome-associated protein (SOP) plays a vital role in stabilizing soy oleosomes owing to its unique amphipathic topological structure. Inspired by the structure of natural oleosomes, in the current study, SOP-decorated liposomes (SOP-Lips) were proposed as a vehicle for improving phospholipid bilayer membrane stability. The micro morphology, size, encapsulation efficiency, and retention rate of SOP-Lips were characterized, the interactions between SOP and the phospholipid bilayer and their effects on the protein and lipid bilayer structures were evaluated. When the liposomes/SOP mass ratio was 1: 0.2 and 1: 0.4, the SOP-Lips exhibited spherical morphology and favorable dispersibility. The quartz crystal microbalance with dissipation monitoring (QCM-D) result suggested that most of SOP bound to liposomes in a tightly integrated way. Spectroscopy analysis indicated that the aromatic amino acids in the protein were exposed to a more hydrophobic microenvironment due to the interactions between the SOP and liposomes. There was an increase in α-helix and decrease in β-sheet and random curl contents in SOP upon exposure to liposomes. The decoration of SOP to liposomes could decrease membrane fluidity and enhance lateral packing of the phospholipid fatty acyl chain. The SOP coating increased the pH, ionic strength and temperature stability of luteolin liposomes (LUT-Lips). In the simulated digestion, SOP-decorated luteolin liposomes (SOP-LUT-Lips) showed a delayed release effect compared with LUT-Lips, suggesting that the inclusion of SOP resulted in a more digestion-resistant structure. This work provides a viable strategy for using SOP-Lips as a delivery system for nutraceuticals in functional food, dietary supplements and pharmaceuticals. • Soybean oleosome-associated protein (SOP) decorated liposomes were constructed. • SOP interacted with liposomes through hydrogen bonding and hydrophobic interaction. • SOP decreased phospholipid membrane fluidity and enhanced the bilayer orderness. • Inclusion of SOP increased the load efficiency of luteolin in liposomes. • SOP modified liposomes exhibited sustained luteolin release profile.