Insight into antioxidant properties of milk‐derived bioactive peptides in vitro and in a cellular model

Tonolo, Federica; Moretto, Laura; Ferro, Stefania; Folda, Alessandra; Scalcon, Valeria; Sandre, Michele; Fiorese, Federico; Marin, Oriano; Bindoli, Alberto; Rigobello, Maria Pia

doi:10.1002/psc.3162

Cited by 28 publications

(17 citation statements)

References 21 publications

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“…Until now, antimicrobial, immunomodulatory, and opioid-like functions, as well as antithrombotic and anti-hypertensive effects, have been reported for bioactive peptides [ 14 , 15 , 16 , 17 ]. Findings indicate that milk peptides can have additional physiological effects, such as antioxidant activity [ 18 ]. They might be able to support growth and bone health as well as immune responses and the cardiovascular system in neonates fed by breast milk [ 19 ].…”

Section: Introductionmentioning

confidence: 99%

Impact of Storage Conditions on the Breast Milk Peptidome

et al. 2020

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Human donor milk (HDM) provides appropriate nutrition and offers protective functions in preterm infants. The aim of the study is to examine the impact of different storage conditions on the stability of the human breast milk peptidome. HDM was directly frozen at −80 °C or stored at −20 °C (120 h), 4 °C (6 h), or room temperature (RT for 6 or 24 h). The milk peptidome was profiled by mass spectrometry after peptide collection by ultrafiltration. Profiling of the peptidome covered 3587 peptides corresponding to 212 proteins. The variance of the peptidome increased with storage temperature and time and varied for different peptides. The highest impact was observed when samples were stored at RT. Smaller but significant effects were still observed in samples stored at 4 °C, while samples showed highest similarity to those immediately frozen at −80 °C when stored at −20 °C. Peptide structures after storage at RT for 24 h point to the increased activity of thrombin and other proteases cleaving proteins at lysine/arginine. The results point to an ongoing protein degradation/peptide production by milk-derived proteases. They underline the need for immediate freezing of HDM at −20 °C or −80 °C to prevent degradation of peptides and enable reproducible investigation of prospectively collected samples.

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Section: Introductionmentioning

confidence: 99%

Impact of Storage Conditions on the Breast Milk Peptidome

et al. 2020

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“…Several protein hydrolysates and peptides with antioxidant effects from animals and plants, such as milk, fish, sesame or wheat brans, hemp or rapeseed, corn, or soy, have been tested both in vitro and in vivo with promising results [18,19,41]. Cell-based systems have also been useful to elucidate the detailed antioxidant mechanism of milk peptides [42,43], fish or seaweed protein hydrolysates [44], and hemp seed or rice endosperm proteins. Nevertheless, only a few studies, including those involving rapeseed hydrolysates, have been assessed in animal models for verifying antioxidant activities in biopeptides [14].…”

Section: Lph Reduces Production Of Ros and Nitrites In Lps-stimulated Thp-1-derived Macrophagesmentioning

confidence: 99%

Antioxidant and Anti-Inflammatory Properties of Bioavailable Protein Hydrolysates from Lupin-Derived Agri-Waste

et al. 2021

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Agri-food industries generate several by-products, including protein-rich materials currently treated as waste. Lupine species could be a sustainable alternative source of protein compared to other crops such as soybean or chickpea. Protein hydrolysates contain bioactive peptides that may act positively in disease prevention or treatment. Inflammatory responses and oxidative stress underlie many chronic pathologies and natural treatment approaches have gained attention as an alternative to synthetic pharmaceuticals. Recent studies have shown that lupin protein hydrolysates (LPHs) could be an important source of biopeptides, especially since they demonstrate anti-inflammatory properties. However, due to their possible degradation by digestive and brush-border enzymes, it is not clear whether these peptides can resist intestinal absorption and reach the bloodstream, where they may exert their biological effects. In this work, the in vitro cellular uptake/transport and the anti-inflammatory and antioxidant properties of LPH were investigated in a co-culture system with intestinal epithelial Caco-2 cells and THP-1-derived macrophages. The results indicate that the LPH crosses the human intestinal Caco-2 monolayer and exerts anti-inflammatory activity in macrophages located in the basement area by decreasing mRNA levels and the production of pro-inflammatory cytokines. A remarkable reduction in nitric oxide and ROS in the cell-based system by peptides from LPH was also demonstrated. Our preliminary results point to underexplored protein hydrolysates from food production industries as a novel, natural source of high-value-added biopeptides.

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“…Samples were analysed for antioxidant capacity through ABTS and DPPH tests [25]. For the first assay, 7 mM ABTS solution and 2.46 mM potassium persulfate were prepared and maintained for 18 h in the dark to obtain the radical molecule ABTS• + .…”

Section: Abts and Dpph Scavengingmentioning

confidence: 99%

Identification of New Peptides from Fermented Milk Showing Antioxidant Properties: Mechanism of Action

et al. 2020

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Due to their beneficial properties, fermented foods are considered important constituents of the human diet. They also contain bioactive peptides, health-promoting compounds studied for a wide range of effects. In this work, several antioxidant peptides extracted from fermented milk proteins were investigated. First, enriched peptide fractions were purified and analysed for their antioxidant capacity in vitro and in a cellular model. Subsequently, from the most active fractions, 23 peptides were identified by mass spectrometry MS/MS), synthesized and tested. Peptides N-15-M, E-11-F, Q-14-R and A-17-E were selected for their antioxidant effects on Caco-2 cells both in the protection against oxidative stress and inhibition of ROS production. To define their action mechanism, the activation of the Kelch-like ECH-associated protein 1/nuclear factor erythroid 2-related factor 2(Keap1/Nrf2) pathway was studied evaluating the translocation of Nrf2 from cytosol to nucleus. In cells treated with N-15-M, Q-14-R and A-17-E, a higher amount of Nrf2 was found in the nucleus with respect to the control. In addition, the three active peptides, through the activation of Keap1/Nrf2 pathway, led to overexpression and increased activity of antioxidant enzymes. Molecular docking analysis confirmed the potential ability of N-15-M, Q-14-R and A-17-E to bind Keap1, showing their destabilizing effect on Keap1/Nrf2 interaction.Antioxidants 2020, 9, 117 2 of 24 proteolysis [3]. Many microorganisms are utilized in this process and it is well known that different fermenting strains can generate various patterns of bioactive peptides [4][5][6]. In particular, for dairy products, Streptococcus thermophilus, Lactobacillus delbrueckii subsp. bulgaricus and Bifidobacterium spp are usually employed [2,7]. Bioactive peptides generated from milk can originate both from whey proteins (β-lactoglobulin, α-lactalbumin, serum albumin, immunoglobulins, lactoferrin and protease-peptone fractions) and from caseins (α-, βand κ-casein) [8][9][10]. Bioactive peptides are studied for their various beneficial activities, for example anti-hypertensive, anti-microbial, opioid and antioxidant [4,[11][12][13][14]. The antioxidant activity of bioactive peptides can depend on their amino acid composition and position in the sequence [15]. Moreover, these compounds can exert their antioxidant activity in cell environment through activation of specific pathways [16,17]. Oxidants and electrophiles are well known molecules recognized to determine the disruption of Keap1/Nrf2 interaction [16,18,19]. However, new series of other compounds are now emerging, such as the bioactive peptides, that with specific protein-protein interactions are able to activate nuclear factor erythroid 2-related factor 2 (Nrf2). The latter, after dissociation from Kelch-like ECH-associated protein 1 (Keap1), migrates to the nucleus where interacts with the antioxidant response element (ARE), activating a large number of genes expressing antioxidant enzymes. Nrf2 translocation is one of the key e...

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Insight into antioxidant properties of milk‐derived bioactive peptides in vitro and in a cellular model

Cited by 28 publications

References 21 publications

Impact of Storage Conditions on the Breast Milk Peptidome

Impact of Storage Conditions on the Breast Milk Peptidome

Antioxidant and Anti-Inflammatory Properties of Bioavailable Protein Hydrolysates from Lupin-Derived Agri-Waste

Identification of New Peptides from Fermented Milk Showing Antioxidant Properties: Mechanism of Action

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