Investigation of the Mechanism of Conformational Alteration in Ovalbumin as Induced by Glycation with Different Monoses through Conventional Spectrometry and Liquid Chromatography High-Resolution Mass Spectrometry

Yang, Yipeng; Liu, Guangxian; Wang, Hui

doi:10.1021/acs.jafc.8b06564

Cited by 37 publications

(36 citation statements)

References 32 publications

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“…The quenching of fluorescence may due to the exposure of aromatic residues (mainly Trp19) into hydrophilic solvents as the conformational structure of the protein gradually unfolds during the glycation progress . This result was also consistent with a previous study: the higher the degree of glycation, the greater the degree of fluorescence quenching . However, the fluorescence intensity of glycated β-Lg containing SeNPs (from 763 to 556 nm) was lower than that of glycated β-Lg without SeNPs (from 935 to 725 nm), because SeNPs had a quenching effect on the fluorescence intensity of native β-Lg.…”

Section: Resultssupporting

confidence: 91%

Mechanism of Selenium Nanoparticles Inhibiting Advanced Glycation End Products

Wang

et al. 2020

J. Agric. Food Chem.

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Selenium nanoparticles (SeNPs) have been applied in fields of nanobiosensors, environment, nanomedicine, etc. as a result of their excellent characteristics. Early studies had shown that SeNPs have certain inhibition ability against glycation, but the inhibition mechanism, especially for the influence of SeNPs on the reaction activity of glycation sites, remains unclear. The aim of the presented research was to reveal the effects of SeNPs on the β-lactoglobulin (β-Lg)/D-ribose glycation system at the molecular level and explore the possible inhibitory mechanism of SeNPs on the formation of advanced glycation end products (AGEs) by analyzing the glycation sites via high-performance liquid chromatography (HPLC)−Orbitrap−tandem mass spectrometry (MS/ MS). Changes in contents of AGE formation and free amino acid contents had indicated that SeNPs could significantly slow the glycation process, thus attenuating the formation of AGEs. HPLC−Orbitrap−MS/MS analysis revealed that, at 6, 12, and 24 h, the number of glycation sites of glycated β-Lg decreased from 7, 7, and 9 to 5, 5, and 6 after the intervention of SeNPs, respectively. The glycation extent of each glycation site was controlled, and the dual-glycation ability of K8, K14, K47, K91, and K101 was changed. All of these results confirmed that SeNPs could indeed slow the process of protein glycation at the molecular level. This may be the reason for SeNPs reducing the formation of AGEs during glycation. Therefore, this study shed light on the insight of how SeNPs reduce the formation of AGEs.

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Section: Resultssupporting

confidence: 91%

Mechanism of Selenium Nanoparticles Inhibiting Advanced Glycation End Products

Wang

et al. 2020

J. Agric. Food Chem.

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“…This suggested that MG-αLA was partially unfolded and reorganized to be a more stable structure. Yang et al (2019) also found similar changes in secondary structures on the investigation of conformational alteration in ovalbumin induced by glycation with different monoses. SDS-PAGE analysis revealed the formation of new dimers, and intrinsic fluorescence analysis also showed the changes in spatial conformation of MG-αLAs.…”

Section: Secondary Structure Analysissupporting

confidence: 65%

Effect of methylglyoxal on the alteration in structure and digestibility of α‐lactalbumin, and the formation of advanced glycation end products under simulated thermal processing

Dong

et al. 2021

Food Science & Nutrition

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α‐Dicarbonyl compounds (α‐DCs) are a class of compounds generated during the thermal processing of food. Due to the high reactivity, α‐DCs were endowed with the ability to react with food components thus lowering nutrition value and even leading to a potential risk for food safety. In this study, methylglyoxal (MG), the most abundant α‐DCs, was selected to investigate the alteration effects on the structure and digestibility of α‐lactalbumin (αLA) under thermal processing (60–100°C). The results showed that the modification degree of αLA by MG increased with the rise of processing temperature, accompanied by the significant changes in molecular weight, intrinsic fluorescence, and secondary structures of αLA. High‐resolution mass spectrometry analysis identified that lysine (Lys) and arginine (Arg) are the modification sites, and Nε‐(carboxyethyl)‐L‐lysine is the main modification type. Since the Lys and Arg are also the cleavage sites of trypsin, the digestibility of MG modified αLA (MG‐αLA) by trypsin correspondingly decreased with an increase of processing temperature. The reacted Lys and Arg residues, and the protein‐bound AGEs were quantified, and the contents were found to be highly dependent on the temperature.

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“…In order to identify the specific protein sites susceptible to SS treatment and explore the mechanism of the decreasing in OVM allergenicity, it is necessary to find out the precise modification sites of OVM. Previous studies have suggested that the antigenic epitopes in protein sequence mainly originated from hydrophobic amino acids and amino acids containing sulfhydryl groups [ 21 , 31 ]. Therefore, trypsin was used to digest native and SS-treated OVM at 120, 140 and 200 °C for 10 min.…”

Section: Resultsmentioning

confidence: 99%

Effects of Superheated Steam Treatment on the Allergenicity and Structure of Chicken Egg Ovomucoid

Wen

et al. 2022

Foods

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The aim of this study was to explore the effects of an emerging and efficient heating technology, superheated steam (SS), on the allergenicity and molecular structure of ovomucoid (OVM). OVM was treated with 120–200 °C of SS for 2 to 10 min. The allergenicity (IgG/IgE binding abilities and cell degranulation assay) and molecular structure (main functional groups and amino acids modification) changes were investigated. The IgG-binding ability of OVM decreased and the releases of β-hex and TNF-γ were inhibited after SS treatment, indicating that the protein allergenicity was reduced. Significant increases in oxidation degree, free SH content and surface hydrophobicity were observed in SS-treated OVM. The protein dimer and trimer appeared after SS treatment. Meanwhile, obvious changes occurred in the primary structure. Specifically, serine can be readily modified by obtaining functional groups from other modification sites during SS treatment. Moreover, the natural OVM structure which showed resistance to trypsin digestion was disrupted, leading to increased protein digestibility. In conclusion, SS-induced OVM aggregation, functional groups and amino acids modifications as well as protein structure alteration led to reduced allergenicity and increased digestibility.

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Investigation of the Mechanism of Conformational Alteration in Ovalbumin as Induced by Glycation with Different Monoses through Conventional Spectrometry and Liquid Chromatography High-Resolution Mass Spectrometry

Cited by 37 publications

References 32 publications

Mechanism of Selenium Nanoparticles Inhibiting Advanced Glycation End Products

Mechanism of Selenium Nanoparticles Inhibiting Advanced Glycation End Products

Effect of methylglyoxal on the alteration in structure and digestibility of α‐lactalbumin, and the formation of advanced glycation end products under simulated thermal processing

Effects of Superheated Steam Treatment on the Allergenicity and Structure of Chicken Egg Ovomucoid

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