The influence of pH and monovalent/divalent cations on the structural and physicochemical properties of myofibrillar protein from silver carp

Wang, Yudong; Zhou, Yang; Yan, Hao; Lü, Yanxuan; Deng, Xingqun; Hu, Yang; Xiong, Shanbai; Yang, Hong

doi:10.1016/j.foodchem.2022.134519

Cited by 19 publications

(5 citation statements)

References 39 publications

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“…Moreover, an increase in the concentration of the MgCl 2 salt did not increase the ThT fluorescence (Figure B), suggesting that the cations with higher valency have no effect in inducing TDP-43 aggregation at low pH. It is plausible that the presence of a divalent cation like Mg 2+ reduces the number of surface hydrophobic interactions or inhibits intermolecular hydrophobic interactions of the MG form. Hence, the presence of a divalent cation like Mg 2+ nullifies the effect of the presence of a higher concentration of a potent anion like Cl – plausibly by interfering with the hydrophobic interactions.…”

Section: Resultsmentioning

confidence: 96%

“…70 The neutralization of the exposed positive charge on the protein by anion binding is the initial step during the salt-induced aggregation of TDP-43 (Figure 6). Surprisingly, ions (Mg 2+ ) that inhibit hydrophobic interactions 55,56 also inhibit the salt-induced aggregation of TDP-43 even in the presence of potent anions (Figure 6). Hence, charge neutralization by anion binding and further hydrophobic interactions are crucial for the salt-induced aggregation of TDP-43 (Figure 8).…”

Section: ■ Discussionmentioning

confidence: 99%

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Electrostatics Choreographs the Aggregation Dynamics of Full-Length TDP-43 via a Monomeric Amyloid Precursor

Doke,

Jha

2024

Biochemistry

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TDP-43 is a ubiquitously expressed, multidomain functional protein that is distinctively known to form aggregates in many fatal neurodegenerative disorders. However, the information for arresting TDP-43 aggregation is missing due to a lack of understanding of the molecular mechanism of the aggregation and structural properties of TDP-43. TDP-43 is inherently prone to aggregation and has minimal protein solubility. Multiple studies have been performed on the smaller parts of TDP-43 or the full-length protein attached to a large solubilization tag. However, the presence of co-solutes or solubilization tags is observed to interfere with the molecular properties and aggregation mechanism of full-length TDP-43. Notably, this study populated and characterized the native, dimeric state of TDP-43 without the interference of co-solutes or protein modifications. We observed that the electrostatics of the local environment is capable of the partial unfolding and monomerization of the native dimeric state of TDP-43 into an amyloidogenic molten globule. By employing the tools of thermodynamics and kinetics, we reveal the structural characteristics and temporal order of the early intermediates and transition states during the transition of the molten globule to β-rich, amyloid-like aggregates of TDP-43, which is governed by the electrostatics of the environment. The current advanced understanding of the nature of native and early aggregation-prone intermediates, early steps, and the influence of electrostatics in TDP-43 aggregation is essential for drug design.

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Section: Resultsmentioning

confidence: 96%

Section: ■ Discussionmentioning

confidence: 99%

Electrostatics Choreographs the Aggregation Dynamics of Full-Length TDP-43 via a Monomeric Amyloid Precursor

Doke,

Jha

2024

Biochemistry

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“…Nevertheless, the emulsifying property of MPs is influenced by many conditions, such as the pH value, ionic strength, and temperature, which may cause a loss of water and fat to deteriorate the stability of emulsified meat products [19]. The pH value of different food systems vary between each other, which not only impacts the taste of the food but also influences the quality characteristics of the products [4].…”

Section: Introductionmentioning

confidence: 99%

Evaluation of the Emulsifying Property and Oxidative Stability of Myofibrillar Protein-Diacylglycerol Emulsions Containing Catechin Subjected to Different pH Values

Li,

Wang,

Zhao

et al. 2024

Foods

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Myofibrillar protein–diacylglycerol emulsions containing catechin (MP-DAG-C) possess outstanding emulsifying property and oxidative stability. However, the effect of pH on MP-DAG-C emulsions should be revealed to provide possibilities for their application in practical meat products. Therefore, MP-DAG-C emulsions at different pH values were used in this study, in which lard, unpurified glycerolytic lard (UGL), and purified glycerolytic lard (PGL) were used as the oil phases. The results indicated that the emulsifying property of the UGL- and PGL-based emulsions increased compared to those of the lard-based emulsions (p < 0.05). The emulsifying activity and stability indices, absolute value of ζ-potential, and rheological characteristics increased with the increase in pH values (p < 0.05), with the droplets were smallest and distributed most uniformly at a pH of 6.5 compared to the other acidic environment (p < 0.05). The thiobarbituric acid substance and carbonyl content increased (p < 0.05), while the total sulfydryl content decreased (p < 0.05) during storage. However, there was no statistical difference between the oxidative stability of the MP-DAG-C emulsions with different pH values (p > 0.05). The results implied that the emulsifying property of MP-DAG-C emulsions increased with an increase in pH values. The oxidative stability of the MP-DAG-C emulsions at high pH values was improved by catechin.

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“…13 Concerning freshwater silver carp, Wang et al recently investigated the influences of pH and salt type on the structural and physicochemical properties of MPs from silver carp, they found that the pH and monovalent/divalent cations could induce various changes in hydrophobic and electrostatic interactions, determining the physicochemical properties of MPs. 14 Xue et al investigated the effect of I on the fishy-odor absorption capacity of MPs from silver carp. 15 However, there has been limited research on the solubility and dissolution characteristics of silver carp MPs and changes in the proteome at different I values.…”

Section: ■ Introductionmentioning

confidence: 99%

Insight into Ionic Strength-Induced Solubilization of Myofibrillar Proteins from Silver Carp (Hypophthalmichthys molitrix): Structural Changes and 4D Label-Free Proteomics Analysis

Li,

Zhang,

Jiao

et al. 2023

J. Agric. Food Chem.

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In this study, changes in the physical, structural, and assembly characteristics of silver carp myofibrillar proteins (MPs) at different ionic strength (I) values were investigated. Moreover, the differential proteomic profile of soluble MPs was analyzed using 4D proteomics based on timsTOF Pro mass spectrometry. Solubility of MPs significantly increased at high I (>0.3), and the increase in I enhanced the apparent viscosity, fluorescence intensity, surface hydrophobicity, and α-helix content of MPs solution. Particle size and sodium dodecyl sulfate-polyacrylamide gel electrophoresis patterns also supported the solubility profiles. Transmission electron microscopy and atomic force microscopy observations revealed the morphological assembly and disassembly of MPs under different I conditions. Finally, proteomic analysis revealed the evolution law of salt-induced solubilization of MPs and the critical molecular characteristics in different I environments. The number of differentially abundant proteins (DAPs) decreased with the increase of I, and most DAPs related to the muscle filament sliding, contraction and assembly, actinin binding, and actin filament binding. The soluble abundance of myosin and some structural proteins was dependent on I, and structural proteins in the Z-disk and M-band might contribute to the solubilization of myosin. Our findings provide insightful information about the impact of common I on the solubility pattern of MPs from freshwater fish.

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The influence of pH and monovalent/divalent cations on the structural and physicochemical properties of myofibrillar protein from silver carp

Cited by 19 publications

References 39 publications

Electrostatics Choreographs the Aggregation Dynamics of Full-Length TDP-43 via a Monomeric Amyloid Precursor

Electrostatics Choreographs the Aggregation Dynamics of Full-Length TDP-43 via a Monomeric Amyloid Precursor

Evaluation of the Emulsifying Property and Oxidative Stability of Myofibrillar Protein-Diacylglycerol Emulsions Containing Catechin Subjected to Different pH Values

Insight into Ionic Strength-Induced Solubilization of Myofibrillar Proteins from Silver Carp (Hypophthalmichthys molitrix): Structural Changes and 4D Label-Free Proteomics Analysis

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