Stabilization of apo α-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study

Radibratović, Milica; Al-Hanish, Ayah; Minić, Simeon; Radomirović, Mirjana; Milčić, Miloš K.; Stanić-Vučinić, Dragana; Veličković, Tanja Ćirković

doi:10.1016/j.foodchem.2018.11.038

Cited by 13 publications

(2 citation statements)

References 39 publications

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“…12,32,33 Under mild conditions, the noncovalent association is usually considered as the fundamental mechanism for phenolic-elicited protein changes. 34,35 Under harsh conditions, e.g., alkaline pH and heating used in the present work, the irreversible covalent interactions would be triggered, and their interactions became more complicated. The formation of covalent bonds involves the auto-oxidation of phenolic compounds and the formation of o-quinones (electron deficient and highly reactive intermediates), which subsequently react with protein nucleophiles in a so-called Michael addition (pathway i in Figure 2).…”

Section: ■ Materials and Methodsmentioning

confidence: 97%

Gallic Acid-Aided Cross-Linking of Myofibrillar Protein Fabricated Soluble Aggregates for Enhanced Thermal Stability and a Tunable Colloidal State

Chen

Liang

et al. 2020

J. Agric. Food Chem.

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Low colloidal stability of myofibrillar protein (MP) during heating is a technofunctional constraint encountered in its beverage application. Gallic acid (GA), a natural polyphenol, was applied to fabricate MP soluble aggregates for an enhanced thermal stability. Upon pH shifting, GA was grafted into MP with the cysteine and tryptophan residues being the binding sites. As a result, the antioxidant activity of MP was enhanced. Additionally, GA modification decreased the α-helix structure of MP and converted MP into cross-linked aggregates. At low dosages (10 and 25 μmol/g GA), disulfide-dominant covalent bonds were formed to generate myosin and actin aggregates, while MP aggregates were mostly bridged through GA−thiols or GA−tryptophan adducts when the dosages exceeded 50 μmol/g. Such aggregates prevented MP from thermal gelation, leading to a stable and tunable colloidal state. This work can foster technological advances in the tailor manufacture of muscle protein-based beverages for special dietary uses.

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Section: ■ Materials and Methodsmentioning

confidence: 97%

Gallic Acid-Aided Cross-Linking of Myofibrillar Protein Fabricated Soluble Aggregates for Enhanced Thermal Stability and a Tunable Colloidal State

Chen

Liang

et al. 2020

J. Agric. Food Chem.

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“…Stabilization of apo-αlactalbumin by binding of epigallocatechin-3-gallate has been observed both with the native and MG states of the former. Binding of epigallocatechin gallate with the MG state of the protein indicated sufficient extent of structural features in the intermediate state to allow binding to the incoming ligand molecules (Radibratovic et al 2019). Formation of the MG state in homodimeric CcD B [controller of cell death B] protein has been characterized spectroscopically (Baliga et al 2019).…”

Section: Recent Qualitative Studies On the Mg Statementioning

confidence: 99%

A look back at the molten globule state of proteins: thermodynamic aspects

Judy

Kishore

2019

Biophys Rev

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Interest in protein folding intermediates lies in their significance to protein folding pathways. The molten globule (MG) state is one such intermediate lying on the kinetic (and sometimes thermodynamic) pathway between native and unfolded states. Development of our qualitative and quantitative understanding of the MG state can provide deeper insight into the folding pathways and hence potentially facilitate solution of the protein folding problem. An extensive look at literature suggests that most studies into protein MG states have been largely qualitative. Attempts to obtain quantitative insights into MG states have involved application of high-sensitivity calorimetry (differential scanning calorimetry and isothermal titration calorimetry). This review addresses the progress made in this direction by discussing the knowledge gained to date, along with the future promise of calorimetry, in providing quantitative information on the structural features of MG states. Particular attention is paid to the question of whether such states share common structural features or not. The difference in the nature of the transition from the MG state to the unfolded state, in terms of cooperativity, has also been addressed and discussed.

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