Key structural factors and intermolecular interactions underlying the formation, functional properties and behaviour in the gastrointestinal tract of the liposomal form of nutraceuticals coated with whey proteins and chitosan.

The aim of this study was to gain a better understanding of the key structural factors and intermolecular interactions underlying the formation, functionality, and gastrointestinal behaviour of the liposomal form of nutraceuticals coated with whey proteins (WPI) and chitosan (CHIT). Phosphatidylcholine (PC) liposomes were used to encapsulate a combination of hydrophobic and hydrophilic nutraceuticals. The hydrophobic constituents were long-chain (LC) n-3 PUFAs (DHA and EPA) from fish oil (FO), vitamin D3, and clove essential oil (CEO), while the hydrophilic component was γ-aminobutyric acid (GABA).

The relationship between the structure and functionality of essential PUFA delivery systems based on sodium caseinate with phosphatidylcholine liposomes without and with a plant antioxidant: an and study.

The aim of this work was to establish the main relationship between the structure and functionality of supramolecular complexes formed by sodium caseinate (SC) with phosphatidylcholine (PC) liposomes filled with fish oil (FO) to an equal mass ratio of n-3 to n-6 polyunsaturated fatty acids (PUFA) in the absence and presence of one of the most effective plant antioxidants, namely the essential oil of clove buds (EOC). The functionality of the supramolecular complexes (SC-PC-FO and SC-PC-FO-EOC) was considered from the point of view of the possibility of their use as effective delivery systems for long-chain n-3 PUFAs (eicosapentaenoic (EPA) and docosahexaenoic (DHA) acids from FO). The laser light scattering method was used in the static, dynamic and electrophoretic modes to characterize the structure and thermodynamic parameters of the supramolecular complexes in an aqueous medium.

Pore formation of phospholipid membranes by the action of two hemolytic arachnid peptides of different size.

Pin2 and Oxki1 are cationic amphipathic peptides that permeate lipid membranes through formation of pores. Their mechanism of binding to phosphocholine (PC) membranes differs. Spin-probe experiments showed that both Pin2 and Oxki1 penetrate the lipid membrane of small unilamellar vesicles (SUVs).