Abstract
In this study, two antioxidant peptides were identified and characterized from the alcalase-hydrolysate of housefly (Musca domestica L.) pupae guided by ABTS cation radical scavenging activity. Peptides sequences were identified as DFTPVCTTELGR (DR12, 1338.48 Da) and ARFEELCSDLFR (AR12, 1485.66 Da) using nano-liquid chromatography-tandem mass spectrometry (LC-MS/MS). Both DR12 and AR12 exert strong ABTS cation radical scavenging ability with EC50 values of 0.39 and 0.35 mM, respectively. Moreover, AR12 can effectively protect PC12 cells from oxidative damage induced by hydrogen peroxide (H2O2) by decreasing intracellular reactive oxygen species (ROS) and malonaldehyde (MDA), recovering cellular mitochondrial membrane potential (MMP), and increasing the activity of intracellular superoxide dismutase (SOD). Stability tests suggest that AR12 is competent for the challenge of heating, acid, alkali or simulated gastrointestinal (GI) digestion and exhibits great activity to remove ABTS cation radical. DR12 shows a great stability against heating, but its antioxidative ability declines after being treated with acid, alkali or simulated GI digestion. In general, both DR12 and AR12 identified from housefly pupae hydrolysate stand a chance of being potential antioxidants or precursors to antioxidants and AR12 might be applied in the field of neuroprotection.
Highlights
IntroductionReactive oxygen species (ROS) are produced during cellular oxygen metabolism and play vital roles in vivo, such as inducing cell differentiation, proliferation and migration, and participating in inter- and intra-cellular signal transmission by stimulating glucose to be transported into cells [1].when the body is suffering from fatigue or illness, the in vivo redox equilibrium could become disrupted, and the excessive accumulation of reactive species would lead to cellular oxidative stress and cause damage to various cellular components, such as membrane structures, DNA or proteins [2,3].This is believed to be a primary cause or a secondary complication of various chronic diseases, e.g., cancer [4], diabetes [5], cardiovascular disease [6,7], rheumatoid arthritis [8], neurodegeneration, and aging process [9,10].In the last two decades, there has been a marked increase in searching for antioxidant peptides from food products, animals or plants resources [11] due to their higher safety and activity compared to synthetic antioxidants, such as butylated hydroxyanisole (BHA) and butylated hydroxytoluene (BHT)which are reported to have latent acute toxicity, developmental [12] and reproductive toxicity [13].Molecules 2019, 24, 4486; doi:10.3390/molecules24244486 www.mdpi.com/journal/moleculesVarious studies have verified that these peptides are usually encrypted in the parent proteins without activity until they are released by various means like fermentation, enzymatic hydrolysis, and curing.For example, Zhu et al identified an antioxidant pentapeptide (Gly-Lys-Phe-Asn-Val) from Jinhua ham, a kind of traditional marinated meat, and this peptide exhibited great radical scavenging activity as well as Fe2+ chelating ability [14]
In the last two decades, there has been a marked increase in searching for antioxidant peptides from food products, animals or plants resources [11] due to their higher safety and activity compared to synthetic antioxidants, such as butylated hydroxyanisole (BHA) and butylated hydroxytoluene (BHT)
These studies that hydrolysis the number of amino acids of20, most antioxidant potent antioxidant peptides were generally enriched in low molecular weight fractions (
Summary
Reactive oxygen species (ROS) are produced during cellular oxygen metabolism and play vital roles in vivo, such as inducing cell differentiation, proliferation and migration, and participating in inter- and intra-cellular signal transmission by stimulating glucose to be transported into cells [1].when the body is suffering from fatigue or illness, the in vivo redox equilibrium could become disrupted, and the excessive accumulation of reactive species would lead to cellular oxidative stress and cause damage to various cellular components, such as membrane structures, DNA or proteins [2,3].This is believed to be a primary cause or a secondary complication of various chronic diseases, e.g., cancer [4], diabetes [5], cardiovascular disease [6,7], rheumatoid arthritis [8], neurodegeneration, and aging process [9,10].In the last two decades, there has been a marked increase in searching for antioxidant peptides from food products, animals or plants resources [11] due to their higher safety and activity compared to synthetic antioxidants, such as butylated hydroxyanisole (BHA) and butylated hydroxytoluene (BHT)which are reported to have latent acute toxicity, developmental [12] and reproductive toxicity [13].Molecules 2019, 24, 4486; doi:10.3390/molecules24244486 www.mdpi.com/journal/moleculesVarious studies have verified that these peptides are usually encrypted in the parent proteins without activity until they are released by various means like fermentation, enzymatic hydrolysis, and curing.For example, Zhu et al identified an antioxidant pentapeptide (Gly-Lys-Phe-Asn-Val) from Jinhua ham, a kind of traditional marinated meat, and this peptide exhibited great radical scavenging activity as well as Fe2+ chelating ability [14]. When the body is suffering from fatigue or illness, the in vivo redox equilibrium could become disrupted, and the excessive accumulation of reactive species would lead to cellular oxidative stress and cause damage to various cellular components, such as membrane structures, DNA or proteins [2,3]. This is believed to be a primary cause or a secondary complication of various chronic diseases, e.g., cancer [4], diabetes [5], cardiovascular disease [6,7], rheumatoid arthritis [8], neurodegeneration, and aging process [9,10]. Three new antioxidant peptides (SVL, EAVQ, and RDY) purified from mulberry (Morus atropurpurea Roxb.) leaf neutrase-hydrolysates displayed great hemolysis inhibition ability and cellular antioxidant activity [16]
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