Improving resveratrol bioavailability using water-in-oil-in-water (W/O/W) emulsion: Physicochemical stability, in vitro digestion resistivity and transport properties

Shi, Aimin; Wang, Jun; Guo, Rui; Feng, Xinyue; Ge, Yanzhen; Liu, Hongzhi; Agyei, Dominic; Wang, Qiang

doi:10.1016/j.jff.2021.104717

Cited by 19 publications

(6 citation statements)

References 39 publications

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“…Thus, most of our simulations are carried out at supersaturated concentrations. Nonetheless, we stress that several chemical 55 and drug delivery strategies 56 have long 57 been discussed to overcome the above limitations.…”

Section: Introductionmentioning

confidence: 99%

Mechanistic Insights into Polyphenols’ Aggregation Inhibition of α-Synuclein and Related Peptides

Martins

Nascimento

Galamba

2023

ACS Chem. Neurosci.

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While several polyphenols were found to either inhibit or modulate the aggregation of proteins implicated in neurodegenerative diseases, such as Parkinson's disease (PD), discrepant action mechanisms have been reported. This, in addition to some polyphenols' pan-assay interference compounds' reputation, casts some doubts concerning their therapeutic relevance. Here, we studied, through molecular dynamics and enhanced sampling methods, the aggregation of 11-mer peptides from the non-amyloid-β component, an aggregation-prone domain of α-synuclein (α-syn) implicated in PD and other synucleinopathies, in neat water and aqueous solutions of resveratrol (RSV) and gallic acid (GA). Further, simulations of the complete protein were carried out in aqueous urea, RSV, and GA solutions. Our results show that peptide aggregation is not disrupted by either phenolic compound. Thus, instead, intrusion of RSV and GA in the inter-peptide region induces a peptide−peptide re-orientation, favoring terminal interactions that manifest in the formation of barrierless solvent-separated configurations. Moreover, although the (poly)phenols induce a pronounced peptide dewetting at high concentrations, β-sheet-rich regions, a hallmark of α-syn aggregation, are not disrupted. Thus, our results indicate that, if anything, RSV and GA delay or modulate peptide aggregation at high concentrations via the stabilization of solvent-separated conformations as opposed to aggregation inhibition. Structural analysis of the full protein, however, shows that the (poly)phenols induce more extended conformations of α-syn, similar to urea, possibly also influencing its aggregation propensity. However, opposite to urea, the (poly)phenols reduce α-syn's conformational space, likely due to steric effects and a slowdown of the solvent dynamics. These effects are concentration-dependent and possibly unattainable at therapeutic-relevant concentrations. These results suggest that the aggregation inhibition activity of RSV and GA in vitro should involve, instead, either the non-covalent binding to oligomeric intermediates or the stabilization of the monomer and/or oligomers through the formation of covalent bonds of the respective quinones with α-syn. In addition, the enhanced aggregation tendency of the peptides observed here could be associated with the formation of non-toxic oligomers, reported for some polyphenols.

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Section: Introductionmentioning

confidence: 99%

Mechanistic Insights into Polyphenols’ Aggregation Inhibition of α-Synuclein and Related Peptides

Martins

Nascimento

Galamba

2023

ACS Chem. Neurosci.

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“…2 C). The introduction of resveratrol may have affected the oil–water interface, leading to a change in the emulsion droplet size ( Shi et al, 2021 ). Meanwhile, the d 4,3 of TWIPNPEs after encapsulating resveratrol increased with increasing TWIPN concentration, similar to the d 4,3 trend of TWIPNPEs before encapsulating resveratrol.…”

Section: Resultsmentioning

confidence: 99%

“…The environment significantly affects the fluorescence spectra of resveratrol, and the hydrophobic interaction between resveratrol and emulsion is determined to identify resveratrol ( Shi et al, 2021 ). The fluorescence spectra of resveratrol in the water phase, soybean oil, and TWIPNPEs are shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

Characteristics and in vitro digestion of resveratrol encapsulated in Pickering emulsions stabilized by tea water-insoluble protein nanoparticles

et al. 2023

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“…Emulsions can be classified according to the spatial organisation of their phases. A system consisting of oil droplets dispersed in an aqueous phase is called an oil-in-water emulsion (O/W), and a system in which water is dispersed in an oil phase is called a water-in-oil emulsion (W/O) [ 17 , 21 , 28 ]. The choice of emulsion system for the protection of functional ingredients depends on the nature of the compound to be protected and the matrix in which the emulsion is to be incorporated.…”

Section: Food Emulsion Formulationmentioning

confidence: 99%

“…Consequently, protection of lipophilic functional ingredients is essential. Protecting of lipophilic functional ingredients via emulsification plays a vital role in increasing the oral bioavailability and providing stability and protection to these compounds [ [16] , [17] , [18] ].…”

Section: Introductionmentioning

confidence: 99%

Emulsification and stabilisation technologies used for the inclusion of lipophilic functional ingredients in food systems

Henao-Ardila,

Quintanilla-Carvajal,

Moreno

2024

Heliyon

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Improving resveratrol bioavailability using water-in-oil-in-water (W/O/W) emulsion: Physicochemical stability, in vitro digestion resistivity and transport properties

Cited by 19 publications

References 39 publications

Mechanistic Insights into Polyphenols’ Aggregation Inhibition of α-Synuclein and Related Peptides

Mechanistic Insights into Polyphenols’ Aggregation Inhibition of α-Synuclein and Related Peptides

Characteristics and in vitro digestion of resveratrol encapsulated in Pickering emulsions stabilized by tea water-insoluble protein nanoparticles

Emulsification and stabilisation technologies used for the inclusion of lipophilic functional ingredients in food systems

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