Modulation of amyloid fibrillation of bovine β-lactoglobulin by selective methionine oxidation

Maity, Sanhita; Sepay, Nayim; Pal, Sampa; Sardar, Subrata; Parvej, Hasan; Pal, Swarnali; Chakraborty, Jishnu; Pradhan, Anirban; Halder, Umesh Chandra

doi:10.1039/d0ra09060c

Cited by 15 publications

(5 citation statements)

References 71 publications

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“…However, it self-aggregates into morphologically distinct fibrils underlining a switch in its interaction capacity. Overall, methionine sulfoxidation is a post-translational modification with significant impact on amyloid aggregation 68 . In this scenario, artificial substitutions of the helical region methionines from the PLD with residues with polar/charged side chains (E/D/S/T/Q/N/K/R) have shown increased cellular toxicity 13 .…”

Section: Discussionmentioning

confidence: 99%

Metamorphism in TDP-43 prion-like domain determines chaperone recognition

et al. 2023

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The RNA binding protein TDP-43 forms cytoplasmic inclusions via its C-terminal prion-like domain in several neurodegenerative diseases. Aberrant TDP-43 aggregation arises upon phase de-mixing and transitions from liquid to solid states, following still unknown structural conversions which are primed by oxidative stress and chaperone inhibition. Despite the well-established protective roles for molecular chaperones against protein aggregation pathologies, knowledge on the determinants of chaperone recognition in disease-related prions is scarce. Here we show that chaperones and co-chaperones primarily recognize the structured elements in TDP-43´s prion-like domain. Significantly, while HSP70 and HSP90 chaperones promote TDP-43 phase separation, co-chaperones from the three classes of the large human HSP40 family (namely DNAJA2, DNAJB1, DNAJB4 and DNAJC7) show strikingly different effects on TDP-43 de-mixing. Dismantling of the second helical element in TDP-43 prion-like domain by methionine sulfoxidation impacts phase separation and amyloid formation, abrogates chaperone recognition and alters phosphorylation by casein kinase-1δ. Our results show that metamorphism in the post-translationally modified TDP-43 prion-like domain encodes determinants that command mechanisms with major relevance in disease.

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Section: Discussionmentioning

confidence: 99%

Metamorphism in TDP-43 prion-like domain determines chaperone recognition

et al. 2023

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“…Bovine β-lactoglobulin forms two types of aggregates in vitro: (1) spherical particles (spherulites [ 212 ]) at pH values near its isoelectric point, and (2) amyloid-like fibrils at pH levels far from the isoelectric point [ 213 ], or under prolonged heating [ 214 ]. The characteristics of the obtained β-lactoglobulin aggregates significantly depend not only on pH and temperature, but also on some other factors, including selective methionine oxidation [ 214 ]. Notably, there is no direct observation of amyloid-like fibrils in milk [ 215 ].…”

Section: The Transition Of β-Barrel Proteins To Amyloidsmentioning

confidence: 99%

β-Barrels and Amyloids: Structural Transitions, Biological Functions, and Pathogenesis

Sulatskaya

Kosolapova

Bobylev

et al. 2021

IJMS

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Insoluble protein aggregates with fibrillar morphology called amyloids and β-barrel proteins both share a β-sheet-rich structure. Correctly folded β-barrel proteins can not only function in monomeric (dimeric) form, but also tend to interact with one another—followed, in several cases, by formation of higher order oligomers or even aggregates. In recent years, findings proving that β-barrel proteins can adopt cross-β amyloid folds have emerged. Different β-barrel proteins were shown to form amyloid fibrils in vitro. The formation of functional amyloids in vivo by β-barrel proteins for which the amyloid state is native was also discovered. In particular, several prokaryotic and eukaryotic proteins with β-barrel domains were demonstrated to form amyloids in vivo, where they participate in interspecies interactions and nutrient storage, respectively. According to recent observations, despite the variety of primary structures of amyloid-forming proteins, most of them can adopt a conformational state with the β-barrel topology. This state can be intermediate on the pathway of fibrillogenesis (“on-pathway state”), or can be formed as a result of an alternative assembly of partially unfolded monomers (“off-pathway state”). The β-barrel oligomers formed by amyloid proteins possess toxicity, and are likely to be involved in the development of amyloidoses, thus representing promising targets for potential therapy of these incurable diseases. Considering rapidly growing discoveries of the amyloid-forming β-barrels, we may suggest that their real number and diversity of functions are significantly higher than identified to date, and represent only “the tip of the iceberg”. Here, we summarize the data on the amyloid-forming β-barrel proteins, their physicochemical properties, and their biological functions, and discuss probable means and consequences of the amyloidogenesis of these proteins, along with structural relationships between these two widespread types of β-folds.

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“…2A) was observed under aggregating conditions indicating the formation of the amyloid fibrillar structure of insulin. 54 The figure demonstrates that the ThT fluorescence intensity started decreasing compared to the heat-treated insulin monomer with a gradual increase of the iron concentration and the minimum ThT intensity was observed when the molar ratio of insulin : Fe 3+ reached 1 : 30, while cupric salt at a relatively lower molar ratio (Ins : Cu = 1 : 3) effectively decreased the ThT fluorescence emission intensity, thus preventing aggregation at a much lower concentration than Fe 3+ (Fig. 2A and C).…”

Section: Resultsmentioning

confidence: 99%

In vitro retardation and modulation of human insulin amyloid fibrillation by Fe³⁺ and Cu²⁺ ions

Paul,

Begum,

Parvej

et al. 2024

New J. Chem.

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Modulation of amyloid fibrillation of bovine β-lactoglobulin by selective methionine oxidation

Abstract: This work reports selective methionine oxidation of β-lactoglobulin by tBHP reduces its thermal stability and enhances fibrillation propensity.

Cited by 15 publications

References 71 publications

Metamorphism in TDP-43 prion-like domain determines chaperone recognition

Metamorphism in TDP-43 prion-like domain determines chaperone recognition

β-Barrels and Amyloids: Structural Transitions, Biological Functions, and Pathogenesis

In vitro retardation and modulation of human insulin amyloid fibrillation by Fe³⁺ and Cu²⁺ ions

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Modulation of amyloid fibrillation of bovine β-lactoglobulin by selective methionine oxidation

Abstract: This work reports selective methionine oxidation of β-lactoglobulin by tBHP reduces its thermal stability and enhances fibrillation propensity.

Cited by 15 publications

References 71 publications

Metamorphism in TDP-43 prion-like domain determines chaperone recognition

Metamorphism in TDP-43 prion-like domain determines chaperone recognition

β-Barrels and Amyloids: Structural Transitions, Biological Functions, and Pathogenesis

In vitro retardation and modulation of human insulin amyloid fibrillation by Fe3+ and Cu2+ ions

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In vitro retardation and modulation of human insulin amyloid fibrillation by Fe³⁺ and Cu²⁺ ions