Structural perturbation by arsenic triggers the aggregation of hen egg white lysozyme by promoting oligomers formation

Varma, Neelakant; Singh, Inderbhan; Dahiya, M. S.; Ravi, Vijay; Kumar, Satish

doi:10.1016/j.ijbiomac.2017.11.096

Cited by 11 publications

(3 citation statements)

References 42 publications

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“…: A Potential Mechanism C3HC4-type RING conformation of PML determines higher selectivity to arsenite (Zhou et al, 2011) (Zhou et al, 2014) (Kaiming et al, 2018). Given that an in vitro experiment demonstrates that the perturbation of secondary structure of protein upon arsenite binding leads to oligomerization (Varma et al, 2018), partial unfolding of the secondary structure of PML protein upon arsenite-binding could trigger oligomerization of PML protein and subsequent nucleation of PML-NBs. Although much remains to be determined, the terminal of the helix in which C77/80, corresponding to i/i+3 arrangements of vicinal cysteines (Cline et al, 2003), locates can be destabilized by arsenite.…”

Section: Arsenite Can Directly Promote Nucleation Of Pml-nbsmentioning

confidence: 99%

How Arsenic, an Inorganic Pollutant, is Involved in the Physiology of Biomolecular Condensates in the Cell

Udagawa

Hirano

2022

Front. Environ. Chem.

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The existence of membrane-less organelles in the cells has been known for a relatively long time. Of the membrane-less organelles, stress granules, processing bodies, and PML-NBs have been intensively investigated in relation to arsenic. The membrane-less organelles, which concentrate biomolecules (proteins, nucleic acids), have recently been shown to self-organize by means of phase separation/transition. These biomolecular condensates (membrane-less organelles) can provide local enhancement of the efficiency of specific reactions. The biomolecular condensates have attracted dramatic attention over the last decade because highly organized biochemical complexes in the cell have long been understood by the membrane-dependent compartmentalization. In this mini review, we highlight the initiation of phase separation for each biomolecular condensate in which arsenic could be involved. We further reflect on the adequacy of the arsenic-dependent ROS levels for the formation of biomolecular condensates. These perspectives led us to re-evaluate the biological action of arsenic from a biophysical and bio-rheological point of view.

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Section: Arsenite Can Directly Promote Nucleation Of Pml-nbsmentioning

confidence: 99%

How Arsenic, an Inorganic Pollutant, is Involved in the Physiology of Biomolecular Condensates in the Cell

Udagawa

Hirano

2022

Front. Environ. Chem.

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“…Recently, Verma et al, showed that the aggregation process of HEWL is also affected by the presence of arsenic trioxide, a metal pollutant. Here, the authors observed that the initial phase of the aggregation process depends on the exposure of hydrophobic surfaces that tend to organize into β-sheet structures [ 76 ].…”

Section: Structural Commonalitiesmentioning

confidence: 99%

Amyloid Prefibrillar Oligomers: The Surprising Commonalities in Their Structure and Activity

Diociaiuti

Bonanni

Cariati

et al. 2021

IJMS

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It has been proposed that a “common core” of pathologic pathways exists for the large family of amyloid-associated neurodegenerations, including Alzheimer’s, Parkinson’s, type II diabetes and Creutzfeldt–Jacob’s Disease. Aggregates of the involved proteins, independently from their primary sequence, induced neuron membrane permeabilization able to trigger an abnormal Ca2+ influx leading to synaptotoxicity, resulting in reduced expression of synaptic proteins and impaired synaptic transmission. Emerging evidence is now focusing on low-molecular-weight prefibrillar oligomers (PFOs), which mimic bacterial pore-forming toxins that form well-ordered oligomeric membrane-spanning pores. At the same time, the neuron membrane composition and its chemical microenvironment seem to play a pivotal role. In fact, the brain of AD patients contains increased fractions of anionic lipids able to favor cationic influx. However, up to now the existence of a specific “common structure” of the toxic aggregate, and a “common mechanism” by which it induces neuronal damage, synaptotoxicity and impaired synaptic transmission, is still an open hypothesis. In this review, we gathered information concerning this hypothesis, focusing on the proteins linked to several amyloid diseases. We noted commonalities in their structure and membrane activity, and their ability to induce Ca2+ influx, neurotoxicity, synaptotoxicity and impaired synaptic transmission.

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“…In vitro studies using fluorescence spectroscopy with thioflavin T and electron microscopy have further demonstrated a dose‐dependent inhibitory effect of myricetin, morin, quercetin, kaempferol, (+)−catechin, and (–)−epicatechin on the formation, extension, and destabilization of β‐AFs at physiological conditions including a pH 7.5 at 37 °C (Ono et al., ). Some food constituents, such as the common environmental pollutant arsenic trioxide can promote self‐assembly of hen egg white lysozyme under physiological conditions (Varma, Singh, Dahiya, Ravi, & Kumar, ).…”

Section: Food Protein Amyloids Potentially Have Negative Health Impacmentioning

confidence: 99%

Rational Design of Amyloid‐Like Fibrillary Structures for Tailoring Food Protein Techno‐Functionality and Their Potential Health Implications

Jansens

Rombouts

Grootaert

et al. 2018

Comp Rev Food Sci Food Safe

124

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To control and enhance protein functionality is a major challenge for food scientists. In this context, research on food protein fibril formation, especially amyloid fibril formation, holds much promise. We here first provide a concise overview of conditions, which affect amyloid formation in food proteins. Particular attention is directed towards amyloid core regions because these sequences promote ordered aggregation. Better understanding of this process will be key to tailor the fibril formation process. Especially seeding, that is, adding preformed protein fibrils to protein solutions to accelerate fibril formation holds promise to tailor aggregation and fibril techno‐functionality. Some studies have already indicated that food protein fibrillation indeed improves their techno‐functionality. However, much more research is necessary to establish whether protein fibrils are useful in complex food systems and whether and to what extent they resist food processing unit operations. In this review the effect of amyloid formation on gelation, interfacial properties, foaming, and emulsification is discussed. Despite their prevalent role as functional structures, amyloids also receive a lot of attention due to their association with protein deposition diseases, prompting us to thoroughly investigate the potential health impact of amyloid‐like aggregates in food. A literature review on the effect of the different stages of the human digestive process on amyloid toxicity leads us to conclude that food‐derived amyloid fibrils (even those with potential pathogenic properties) very likely have minimal impact on human health. Nevertheless, prior to wide‐spread application of the technology, it is highly advisable to further verify the lack of toxicity of food‐derived amyloid fibrils.

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Structural perturbation by arsenic triggers the aggregation of hen egg white lysozyme by promoting oligomers formation

Cited by 11 publications

References 42 publications

How Arsenic, an Inorganic Pollutant, is Involved in the Physiology of Biomolecular Condensates in the Cell

How Arsenic, an Inorganic Pollutant, is Involved in the Physiology of Biomolecular Condensates in the Cell

Amyloid Prefibrillar Oligomers: The Surprising Commonalities in Their Structure and Activity

Rational Design of Amyloid‐Like Fibrillary Structures for Tailoring Food Protein Techno‐Functionality and Their Potential Health Implications

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