Engineering marine phospholipid nanoliposomes via glycerol-infused proliposomes: Mechanisms, strategies, and versatile applications in scalable food-grade nanoliposome production.

This study presents a novel approach using polyol-based proliposome to produce marine phospholipids nanoliposomes. Proliposomes were formulated by blending glycerol with phospholipids across varying mass ratios (2:1 to 1:10) at room temperature. Analysis employing polarized light microscopy, FTIR, and DSC revealed that glycerol disrupted the stacked acyl groups within phospholipids, lowering the phase transition temperature (Tm). Krill oil phospholipids (KOP) proliposomes exhibited superior performance in nanoliposomes formation, with a mean diameter of 125.60 ± 3.97 nm, attributed to the decreased Tm (-7.64 and 7.00 °C) compared to soybean phospholipids, along with a correspondingly higher absolute zeta potential (-39.77 ± 1.18 mV). The resulting KOP proliposomes demonstrated liposomes formation stability over six months and under various environmental stresses (dilution, thermal, ionic strength, pH), coupled with in vitro absorption exceeding 90 %. This investigation elucidates the mechanism behind glycerol-formulated proliposomes and proposes innovative strategies for scalable, solvent-free nanoliposome production with implications for functional foods and pharmaceutical applications.

Stability of resveratrol esters with caprylic acid during simulated in vitro gastrointestinal digestion.

Lipophenols, esterified phenols with fatty acids, have attracted increasing attention because of their better protective effects in lipid-based food matrices from oxidation. However, little is known about their digestion. In this study, the digestive stability of resveratrol (RSV) esters with caprylic acid (RCAPs) in a model gastrointestinal digestion system was evaluated. The results demonstrated that RCAPs were relatively stable without hydrolysis in mouth and gastric phases. However, in the intestinal phase, pancreatic lipase rather than phospholipase A2 could hydrolyze monoester and diesters to free RSV. After 120 min of incubation at 37 °C, 53.68% of monoester and 11.36% of diesters were hydrolyzed. However, no hydrolysis of the triester was noticed. Obviously, the level of hydrolysis of RCAPs was negatively correlated with the degree of substitution. Therefore, it was speculated that RSV in fatty acid ester forms could partially be absorbed by intestinal lumen in the form of free RSV.

Cyclic RGD functionalized liposomes encapsulating urokinase for thrombolysis.

Thrombosis, a critical event in blood vessels, not only is associated with myocardial infarction and stroke, but also accounts for considerable morbidity and mortality. Thrombolytic drugs are usually applied to the treatment of acute myocardial infarction, acute cerebral infarction and pulmonary embolism. However, thrombolytic drugs show limited efficacy in clinical practice because of the short half-life in plasma and systemic side effects. In this study, the cyclic RGD (cRGD) functionalized liposomes were prepared to encapsulate urokinase, a cheap and widely used thrombolytic drug in clinic and better thrombolysis efficacy was achieved. The flow cytometry analysis showed that the cRGD liposomes could bind to the activated platelets while not to the resting platelets. In vitro release study revealed that the release percentage reached plateau in about 5 h with 60% urokinase being released from liposomes. Results from the in vitro thrombolysis experiments demonstrated a good thrombolysis potential of the cRGD urokinase liposomes. The in vivo thrombolysis study demonstrated that the cRGD liposomes could significantly reduce the dose of urokinase by 75% while achieving the equivalent thrombolysis effect as the free urokinase in mouse mesenteric thrombosis model. In conclusion, the cRGD liposomes encapsulating urokinase hold great promise in clinic for better thrombolytic efficacy. STATEMENT OF SIGNIFICANCE: In this paper, the cRGD liposomes were prepared to encapsulate urokinase for targeted thrombolysis therapy. The cRGD liposomes could specifically bind to the activated platelets and could stably and continuously release its loaded urokinase. The mouse mesenteric thrombosis model was established to evaluate the thrombolysis effect of the cRGD urokinase liposomes. The results demonstrated that the cRGD liposomes could improve the thrombolytic efficacy by almost 4-fold over free urokinase. In conclusion, the cRGD liposomes encapsulating urokinase had great potential for the clinical treatment of thrombosis.