Interactions of epigallo-catechin 3-gallate and ovalbumin, the major allergen of egg white

Ognjenović, Jana; Stojadinovic, Marija; Milčić, Miloš K.; Apostolović, Danijela; Vesic, Jelena; Stambolic, Ivan; Atanasković-Marković, Marina; Simonović, Miljan; Veličković, Tanja Ćirković

doi:10.1016/j.foodchem.2014.05.005

Cited by 75 publications

(39 citation statements)

References 38 publications

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“…S-11). In conclusion, these and previously published results point to EGCG as a generic binder [34][35][36][37][38][39][40][41][42] and modulator 41,42 of protein structure.…”

Section: Egcg Binding Promotes As Compactionsupporting

confidence: 79%

Opposite Structural Effects of Epigallocatechin-3-gallate and Dopamine Binding to α-Synuclein

et al. 2016

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The intrinsically disordered and amyloidogenic protein -synuclein (AS) has been linked to several neurodegenerative states, including Parkinson's disease. Here, nano-electrospray-ionization mass spectrometry (nano-ESI-MS), ion mobility (IM), and native top-down electron transfer dissociation (ETD) techniques are employed to study AS interaction with small molecules known to modulate its aggregation, such as epigallocatechin-3-gallate (EGCG) and dopamine (DA). The complexes formed by the two ligands under identical conditions reveal peculiar differences. While EGCG engages AS in compact conformations, DA preferentially binds to the protein in partially extended conformations. The two ligands also have different effects on AS structure as assessed by IM, with EGCG leading to protein compaction and DA to its extension. Native top-down ETD on the protein-ligand complexes shows how the different observed modes of binding of the two ligands could be related to their known opposite effects on AS aggregation. The results also show that the protein can bind either ligand in the absence of any covalent modifications, such as e.g. oxidation.

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“…S-11). In conclusion, these and previously published results point to EGCG as a generic binder [34][35][36][37][38][39][40][41][42] and modulator 41,42 of protein structure.…”

Section: Egcg Binding Promotes As Compactionsupporting

confidence: 79%

Opposite Structural Effects of Epigallocatechin-3-gallate and Dopamine Binding to α-Synuclein

et al. 2016

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“…() demonstrated that the formation of α‐lactalbumin and epigalocatechin‐3‐gallate (ECGC) complex results in typical exothermic enthalpy change (20 m m phosphate buffer, pH 7.2). Such phenomenon was also observed upon binding of ECGC to lipase (Wu et al ., ), BSA, β‐casein and porcine gelatin (Bohin et al ., ), ovalbumin (Ognjenovic et al ., ), insulin (Wang et al ., ), keratin (Zhao et al ., ), catalase (Pal et al ., ) and Ara h 2 and Ara h 6 proteins (Vesic et al ., ). In the case of Ara h 2 and Ara h 6 proteins, the formation of complex was accompanied by exothermic enthalpy changes (20 m m sodium phosphate, pH 7.2).…”

Section: Thermodynamic Methodsmentioning

confidence: 99%

A review of methods used for investigation of protein–phenolic compound interactions

Czubiński

Dwiecki

2016

Int J of Food Sci Tech

151

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Interactions between the different compounds present in foods are common and have influence on the nutritional and functional properties of food products. Among a wide range of these interactions, the formation of complexes between proteins and phenolic compounds seems to be the most important issue. Complexation of the phenolic compounds with proteins can be analysed considering several aspects. These complexes might strongly affect nutritional potential of polyphenols by masking their antioxidant capacity, and on the other hand might have influence on the structure of proteins which may cause their precipitation or decrease susceptibility to digestion. The complexity of protein–phenolic compound interactions is a challenge for food analysts and forced researchers to establish a wide range of analytical methods, allowing determination of complexes formation. The main aim of this review is to give researchers an overview of the currently used methods that can be applied to study the interactions between proteins and phenolic compounds.

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“…As shown in Figure 1b, the emission peak of myofibril protein had an obvious red shift from 336 to 341 nm with the increasing concentration of EGCG, which indicated that EGCG could change the tertiary structure of myofibril protein, and then, further enhance its hydrophily. It has been reported that the change of spatial structure may cause the exposure of more amino acid residues to the hydrophilic environment, and accelerate the disintegration of hydrophobic structure of protein, which are meaningful for the improvement of tenderness of meat (Chen, Wang, Feng, Jiang, & Miao, 2019; Ognjenović et al, 2014).…”

Section: Resultsmentioning

confidence: 99%

Effect of tea polyphenols on the tenderness of yak meat

Gao

Zeng

2020

J Food Process Preserv

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The effect and action mechanism of tea polyphenols (TP) on the tenderness of yak meat were investigated. With the treatment of TP at the low concentrations, the myofibril fragmentation index (MFI) value of yak meat was increased and its microstructure was obviously changed. By using fluorescence spectroscopy and the determination of surface hydrophobicity, the tertiary structure of myofibrillar protein (MP) showed the obvious changes with the treatment of epigallocatechin gallate (EGCG). In addition, the secondary structure of MP was also obviously changed according to the measurement of circular dichroism (CD) spectrum, while the α‐helix structure of MP decreased and the β‐sheet increased. Furthermore, according to the analysis of molecular docking, EGCG could interact tightly with myofibril protein by hydrogen bonds, and changed its spatial configuration and molecular force. All results suggested that TPs showed the potentially value to improve the tenderness of yak meat in food industry. Practical applications Yak meat is more and more popular by its high nutrition value. But due to its special myofibril protein, the tenderness of yak meat is unfavorably and affects its sensory properties, which may limit its processing and consumption in food industry. In present study, TPs was used to improve the tenderness of yak meat by changing the spatial configuration and molecular force of myofibril protein, which suggested that TPs showed the potential value to enhance the quality of yak meat during its processing in food industry.

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Interactions of epigallo-catechin 3-gallate and ovalbumin, the major allergen of egg white

Cited by 75 publications

References 38 publications

Opposite Structural Effects of Epigallocatechin-3-gallate and Dopamine Binding to α-Synuclein

Opposite Structural Effects of Epigallocatechin-3-gallate and Dopamine Binding to α-Synuclein

A review of methods used for investigation of protein–phenolic compound interactions

Effect of tea polyphenols on the tenderness of yak meat

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