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Tau is a natively unfolded microtubule-associated protein. Tau neurofibrillary tangles are one of the hallmarks of Alzheimer's disease. The post-translational modifications of Tau lead to its pathological state. Phosphorylation is the key post-translational modification associated with Tauopathy. Curcumin is a polyphenolic compound present in the rhizomes of Curcuma longa. Curcumin has been reported to have remarkable medicinal properties in several diseases, but its poor solubility limits its therapeutic potency. Artemisinin is a sesquiterpene lactone, which has been known sience ancient times for its applications as a treatment for various diseases such as malaria, cancer, autoimmune disease, etc. In the present study, the potency of crystalline curcumin, crystalline artemisinin, and Cur-Art co-amorphous dispersion were evaluated against Tau pathology. The in-vitro ThS/ANS fluorescence and electron microscopy results suggested that curcumin and Cur-Art efficiently inhibited Tau aggregation. Furthermore, exposure to curcumin and Cur-Art co-amorphous restored the impaired nuclear transport in formaldehyde-stressed cells. Curcumin was also found to modulate the phosphorylation of Tau, which indicated the neuroprotective potency. Thus, curcumin and Cur-Art co-amorphous exhibit therapeutic potential against Tau protein in Alzheimer's disease., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2022 Elsevier B.V. All rights reserved.)

Chapatti is a flattened circular flatbread also known as roti, poli, safari, and phulka, usually baked on a hot iron griddle. It is a staple diet of India and hence the quality of chapatti plays a major role in its acceptance. The overall quality of chapatti is dependent on various attributes such as pliability, handfeel, chapatti eating quality, and taste. These attributes are influenced by numerous factors, including wheat genotypes, wheat varieties, the molecular weight distribution of proteins, and processing techniques . This staple food has been extensively studied for various aspects, including processing, mechanism, fractionation, and reconstitution, quality improver, shelf life extension and also the mechanization of processing. This review focus on all the above-mentioned aspects and innovations carried out in this area., Competing Interests: Conflict of interestThere is no conflict of interest by all authors., (© Association of Food Scientists & Technologists (India) 2020.)

Background: Alzheimer's disease is a type of dementia denoted by progressive neuronal death due to the accumulation of proteinaceous aggregates of Tau. Post-translational modifications like hyperphosphorylation, truncation, glycation, etc . play a pivotal role in Tau pathogenesis. Glycation of Tau aids in paired helical filament formation and abates its microtubule-binding function. The chemical modulators of Tau PTMs, such as kinase inhibitors and antibody-based therapeutics, have been developed, but natural compounds, as modulators of Tau PTMs are not much explored., Materials and Methods: We applied biophysical and biochemical techniques like fluorescence kinetics, oligomerization analysis and transmission electron microscopy to investigate the impact of EGCG on Tau glycation in vitro . The effect of glycation on cytoskeleton instability and its EGCG-mediated rescue were studied by immunofluorescence microscopy in neuroblastoma cells., Results: EGCG inhibited methyl glyoxal (MG)-induced Tau glycation in vitro . EGCG potently inhibited MG-induced advanced glycation endproducts formation in neuroblastoma cells as well modulated the localization of AT100 phosphorylated Tau in the cells. In addition to preventing the glycation, EGCG enhanced actin-rich neuritic extensions and rescued actin and tubulin cytoskeleton severely disrupted by MG. EGCG maintained the integrity of the Microtubule Organizing Center (MTOC) stabilized microtubules by Microtubule-associated protein RP/EB family member 1 (EB1)., Conclusions: We report EGCG, a green tea polyphenol, as a modulator of in vitro methylglyoxal-induced Tau glycation and its impact on reducing advanced glycation end products in neuroblastoma cells. We unravel unprecedented function of EGCG in remodeling neuronal cytoskeletal integrity., Competing Interests: CONFLICTS OF INTEREST Authors have no conflicts of interest to declare., (Copyright: © 2021 Sonawane and Chinnathambi.)

Background: Microtubule-associated protein Tau undergoes aggregation in Alzheimer`s disease (AD) and a group of other related diseases collectively known as Tauopathies. In AD, Tau forms aggregates, which are deposited intracellularly as neurofibrillary tangles. Histone deacetylase-6 (HDAC6) plays an important role in aggresome formation, where it recruits polyubiquitinated aggregates to the motor protein dynein., Methods: Here, we have studied the effects of HDAC6 ZnF UBP on Tau phosphorylation, ApoE localization, GSK-3β regulation and cytoskeletal organization in neuronal cells by immunocytochemical analysis. This analysis reveals that the cell exposure to the UBP-type zinc finger domain of HDAC6 (HDAC6 ZnF UBP) can modulate Tau phosphorylation and actin cytoskeleton organization., Results: HDAC6 ZnF UBP treatment to cells did not affect their viability and resulted in enhanced neurite extension and formation of structures similar to podosomes, lamellipodia and podonuts suggesting the role of this domain in actin re-organization. Also, HDAC6 ZnF UBP treatment caused increase in nuclear localization of ApoE and tubulin localization in microtubule organizing centre (MTOC). Therefore, our studies suggest the regulatory role of this domain in different aspects of neurodegenerative diseases. Upon HDAC6 ZnF UBP treatment, inactive phosphorylated form of GSK-3β increases without any change in total GSK-3β level., Conclusions: HDAC6 ZnF UBP was found to be involved in cytoskeletal re-organization by modulating actin dynamics and tubulin localization. Overall, our study suggests that ZnF domain of HDAC6 performs various regulatory functions apart from its classical function in aggresome formation in protein misfolding diseases. Video abstract.

The objective of the study was to screen amongst various gluten free flours to prepare Indian unleavened flatbread using principal component analysis (PCA) and hierarchical cluster analysis (HCA) as a mathematical tool. Gluten free flours studied in this work were, rice, sorghum, moong, amaranth, sama, ragi, water chestnut, buckwheat, soy, tamatind kernel, chickpea, black gram and unripe banana flour. The characteristics of sorghum: rice flatbread was analyzed such as dough making ability, subjective rollability, puffing and acceptability with respect to wheat. Interrelationship between the parameters analyzed and the different gluten free flours were investigated by using PCA and HCA. PCA revealed that the first two components represented 92.56% of the total variability in flatbread making characteristics. HCA classified samples into 6 clusters on the basis of measured flatbread making characteristics. From the results, moong, water chestnut and unripe banana flour in addition to mixture sorghum: rice (30:70) flour were chosen as ingredients for the preparation of Indian unleavened flatbread., Competing Interests: Conflict of interestAll authors in the manuscript do not have any conflict of interest., (© Association of Food Scientists & Technologists (India) 2020.)

Aloe vera catches attention of food industry due to its various health benefits like emollient, anti-inflammatory, purgative, anti-microbial, aphrodisiac, antifungal, and antioxidant. Aloe vera gel has excellent functional and nutritional properties and its incorporation into food can increase its functional and nutritional value of the food. However, both the pulp and aloe gel contain a lot of insoluble polymer particles, which affect the rheological behaviour and physical stability mechanisms of the suspensions during storage and processing. While many researchers have explored the application of aloe vera juice in the food products, no literature review of food applications of aloe vera along with their rheological properties have been complied. Hence, the present review aimed to focus on the utilization of aloe vera in the various sectors of food processing and gives insights on the rheological and flow behaviour of aloe vera juice which is a critical parameter for its food application., (© Association of Food Scientists & Technologists (India) 2020.)

Background: Amyloid aggregate deposition is the key feature of Alzheimer's disease. The proteinaceous aggregates found in the afflicted brain are the intra-neuronal neurofibrillary tangles formed by the microtubule-associated protein Tau and extracellular deposits, senile plaques, of amyloid beta (Aβ) peptide proteolytically derived from the amyloid precursor protein. Accumulation of these aggregates has manifestations in the later stages of the disease, such as memory loss and cognitive inabilities originating from the neuronal dysfunction, neurodegeneration, and brain atrophy. Treatment of this disease at the late stages is difficult, and many clinical trials have failed. Hence, the goal is to find means capable of preventing the aggregation of these intrinsically disordered proteins by inhibiting the early stages of their pathological transformations. Polyphenols are known to be neuroprotective agents with the noticeable potential against many neurodegenerative diseases, such as Alzheimer's, Parkinson's, and Prion diseases., Methods: We analyzed the capability of Baicalein to inhibit aggregation of human Tau protein by a multifactorial analysis that included several biophysical and biochemical techniques., Results: The potency of Baicalein, a polyphenol from the Scutellaria baicalensis Georgi, against in vitro Tau aggregation and PHF dissolution has been screened and validated. ThS fluorescence assay revealed the potent inhibitory activity of Baicalein, whereas ANS revealed its mechanism of Tau inhibition viz. by oligomer capture and dissociation. In addition, Baicalein dissolved the preformed mature fibrils of Tau thereby possessing a dual target action. Tau oligomers formed by Baicalein were non-toxic to neuronal cells, highlighting its role as a potent molecule to be screened against AD., Conclusion: In conclusion, Baicalein inhibits aggregation of hTau40 by enhancing the formation of SDS-stable oligomers and preventing fibril formation. Baicalein-induced oligomers do not affect the viability of the neuroblastoma cells. Therefore, Baicalein can be considered as a lead molecule against Tau pathology in AD. Video Abstract.

In this era of green technology, plasma technology is one of the novel techniques intended towards many industries including food industry as a principal application due to less utilization of energy, solvents, and water with minimum impact on food quality. The foremost purpose behind the utilization of nonthermal plasma processing (cold plasma) lies in the retention of freshness of food products along with furtherance of sensory properties as well as functional and nutritional composition. In addition, this technique assists in shelf life extension and carries out desirable modifications in the structure of food and packaging material. This technology has been proven to be advantageous over other technologies since all these processes are carried out at low temperature, hence is highly suitable for heat-sensitive materials. The present review summarizes the mechanism of this plasma technology along with its benefits to the industry, for example improvements in cooking quality, enhancements in enzyme activity, modification of starches, and microbial inactivation. Also, the effects of plasma treatment on characteristics of various food products have been elaborated in this review.

In this study, the rheological properties of dough prepared from gluten free flours (rice, sorghum, moong, water chestnut and unripe banana) and wheat dough were determined. Pasting properties and viscoelastic properties were analyzed using rheometer and dough rheology experiment was performed on texture analyzer. Water chestnut flour exhibited highest peak viscocity (22.6 Pa s), trough viscosity (12.1), breakdown viscosity (10.5 Pa s) and final viscosity (14.92 Pa s) than others while unripe banana flour showed highest setback viscosity (4.54 Pa s). Pasting temperature was found to be highest for sorghum followed by wheat and others. The highest elastic (G') and loss (G″) module were obtained for moong flour. Wheat and gluten free flours were found to exhibit thixotropic effect. Moong flour dough was found to be the stickiest (dough stickiness 57.83 g) followed by WCF, UBF, wheat, rice and sorghum. Similar trend was observed for dough strength. These flours can be proved as key materials for the gluten-free products market and can provide additional inexpensive advantage to the food processing industry., Competing Interests: Conflict of interestAuthors do not have any conflict., (© Association of Food Scientists & Technologists (India) 2020.)

Tau aggregation and accumulation is a key event in the pathogenesis of Alzheimer's disease. Inhibition of Tau aggregation is therefore a potential therapeutic strategy to ameliorate the disease. Phytochemicals are being highlighted as potential aggregation inhibitors. Epigallocatechin-3-gallate (EGCG) is an active phytochemical of green tea that has shown its potency against various diseases including aggregation inhibition of repeat Tau. The potency of EGCG in altering the PHF assembly of full-length human Tau has not been fully explored. By various biophysical and biochemical analyses like ThS fluorescence assay, MALDI-TOF analysis and Isothermal Titration Calorimetry, we demonstrate dual effect of EGCG on aggregation inhibition and disassembly of full-length Tau and their binding affinity. The IC50 for Tau aggregation by EGCG was found to be 64.2 μM.

In Alzheimer's disease and related tauopathies, the aggregation of microtubule-associated protein, Tau, into fibrils occurs via the interaction of two hexapeptide motifs PHF* 275 VQIINK 280 and PHF 306 VQIVYK 311 as β-sheets. To understand the role of the constituent amino acids of PHF and PHF* in the aggregation, a set of 12 alanine mutant peptides was synthesized by replacing each amino acid in PHF and PHF* with alanine and they were characterized by nuclear magnetic resonance (NMR) spectroscopy, circular dichroism (CD), transmission electron microscopy (TEM) and ThS/ANS fluorescence assay. Our studies show that while the aggregation was suppressed in most of the alanine mutant peptides, replacement of glutamine by alanine in both PHF and PHF* enhanced the fibrillization., Competing Interests: There are no conflicts to declare., (This journal is © The Royal Society of Chemistry.)

Background: Frontotemporal dementia and parkinsonism-linked to chromosome-17 are a group of diseases with tau mutations leading to primary tauopathies which include progressive supranuclear palsy, corticobasal syndrome, and frontotemporal lobar degeneration. Alzheimer's disease is a non-primary tauopathy, which displays tau neuropathology of excess tangle formation and accumulation. FTDP-17 mutations are responsible for early onset of AD, which can be attributed to compromised physiological functions due to the mutations. Tau is a microtubule-binding protein that secures the integrity of polymerized microtubules in neuronal cells. It malfunctions owing to various insults and stress conditions-like mutations and post-translational modifications., Objective: In this study, we modified the wild type and tau mutants by methyl glyoxal and thus studied whether glycation can enhance the aggregation of predisposed mutant tau., Methods: Tau glycation was studied by fluorescence assays, SDS-PAGE analysis, conformational evaluation, and transmission electron microscopy., Results: Our study suggests that FTDP-17 mutant P301 L leads to enhanced glycation-induced aggregation as well as advanced glycation end products formation. Glycation forms amorphous aggregates of tau and its mutants without altering its native conformation., Conclusion: The metabolic anomalies and genetic predisposition have found to accelerate tau-mediated neurodegeneration and prove detrimental for the early-onset of Alzheimer's disease.

Alzheimer's disease (AD) is a neurodegenerative disorder caused by protein misfolding, aggregation and accumulation in the brain. A large number of molecules are being screened against these pathogenic proteins but the focus for therapeutics is shifting towards the natural compounds as aggregation inhibitors, mainly due to their minimum adverse effects. Baicalein is a natural compound belonging to the class of flavonoids isolated from the Chinese herb Scutellaria baicalensis. Here we applied fluorescence, absorbance, microscopy, MALDI-TOF spectrophotometry and other biochemical techniques to investigate the interaction between Tau and Baicalein in vitro. We found the aggregation inhibitory properties of Baicalein for the repeat Tau. Overall, the potential of Baicalein in dissolving the preformed Tau oligomers as well as mature fibrils can be of utmost importance in therapeutics for Alzheimer's disease., (Copyright © 2019. Published by Elsevier Inc.)

The Alzheimer's disease (AD) therapeutic research is yielding a large number of potent molecules. The nanoparticle-based therapeutics against the protein aggregation in AD is also taking a lead especially with amyloid-β as a primary target. In this work, we have screened for the first time protein-capped (PC) metal nanoparticles for their potency in inhibiting Tau aggregation in vitro. We present a novel function of PC-Fe 3 O 4 and PC-CdS nanoparticles as potent Tau aggregation inhibitors by fluorescence spectrometry, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and electron microscopy. We demonstrate that the biologically synthesized PC-metal nanoparticles, especially iron oxide do not affect the viability of neuroblastoma cells. Moreover, PC-CdS nanoparticles show dual properties of inhibition and disaggregation of Tau. Thus, the nanoparticles can take a lead as potent Tau aggregation inhibitors and can be modified for specific drug delivery due to their very small size. The current work presents unprecedented strategy to design anti-Tau aggregation drugs, which provides interesting insights to understand the role of biological nanostructures in Alzheimer's disease., Competing Interests: The authors declare no competing financial interest.

Recently, a novel technique for extraction of functional thermally sensitive bioactive components from food has been developed due to its green efficacy (no toxic chemicals) and cost effectiveness. Cloud point extraction (CPE) is one of the such best alternative techniques that can be used for extraction of wide range of organic and inorganic components using green surfactants. It is a simple, rapid and inexpensive extraction technique which involves clustering of non-ionic surfactant monomers to form a hydrophobic core (micelle), which then entraps the hydrophobic bioactive compounds within it. CPE can be applied for extraction of bioactives from food processing waste as well as separation and purification of proteins. Besides that, research has received special attention on sample preparation for analysis of food constituents in the last decade. The scope of CPE is very vast in these sectors because of the advantages of CPE over other methods. This review deals with significance of CPE method and their potential green applications in food processing., Competing Interests: Compliance with ethical standardsAuthors have declared that no conflict of interest exist.

The microtubule-associated protein Tau plays a key role in the neuropathology of Alzheimer's disease by forming intracellular neurofibrillary tangles. Tau in the normal physiological condition helps stabilize microtubules and transport. Tau aggregates due to various gene mutations, intracellular insults and abnormal post-translational modifications, phosphorylation being the most important one. Other modifications which alter the function of Tau protein are glycation, nitration, acetylation, methylation, oxidation, etc. In addition to forming intracellular aggregates, Tau pathology might spread in a prion-like manner as revealed by several in vitro and in vivo studies. The possible mechanism of Tau spread can be via bulk endocytosis of misfolded Tau species. The recent studies elucidating this mechanism have mainly focussed on the aggregation and spread of repeat domain of Tau in the cell culture models. Further studies are needed to elucidate the prion-like propagation property of full-length Tau and its aggregates in a more intense manner in vitro as well as in vivo conditions. Varied post-translational modifications can have discrete effects on aggregation propensity of Tau as well as its propagation. Here, we review the prion-like properties of Tau and hypothesize the role of glycation in prion-like properties of Tau. This post-translationally modified Tau might have an enhanced propagation property due to differential properties conferred by the modifications.

Tamarind seed has been a source of valuable nutrients such as protein (contains high amount of many essential amino acids), essential fatty acids, and minerals which are recognized as additive to develop perfect balanced functional foods. The objective of present work was to optimize the process parameters for extraction and hydrolysis of protein from tamarind seeds. Papain-derived hydrolysates showed a maximum degree of hydrolysis (39.49%) and radical scavenging activity (42.92 ± 2.83%) at optimized conditions such as enzyme-to-substrate ratio (1:5), hydrolysis time (3 h), hydrolysis temperature (65 °C), and pH 6. From this study, papain hydrolysate can be considered as good source of natural antioxidants in developing food formulations., Competing Interests: Compliance with ethical standardsAuthors do not have any conflict of interest.

This study examines the extraction and hydrolysis of proteins using single factor and Box-Behnken Design (BBD). From single factor tests, optimised extraction parameters were 1% alkali concentration, 40 °C temperature, 60 min time, and 1:20 solid to alkali ratio. Under these conditions; 924.31 mg/g of total protein was obtained from Limonia acidissima (L acidissima). The maximum degree of hydrolysis was 39.82% at pH 2, enzyme to substrate ratio 2.5% (w/w), and hydrolysis time was 42.41 min using BBD design. L acidissima seed protein hydrolysate showed 32.94% DPPH and 88.18% of ABTS activity at concentration of 100 µg/ml and 1 mg/ml, respectively. Reducing power of 0.16 and metal chelating activity of 87.39% was obtained from 5 mg/ml protein hydrolysates. This implied that L acidissima seed protein hydrolysate could be utilised in protein rich product or as protein supplements.

Jambhul and wood apple were subjected to two different drying methods to examine the effect of drying temperatures (80 °C and 60 °C) and influence of storage conditions viz., room temperature (25 °C) and refrigeration temperature (4 °C) on bioactive constituents of jambhul and wood apple powder for 90 days. Results showed that retention of phenolics, ascorbic acid and antioxidant capacity such as ABTS, DPPH and FRAP in jambhul and wood apple were high at 80 °C as compared to 60 °C in both tray and IR drying. Anthocyanin and flavonoid significantly (p < 0.05) decreased at 80 °C. Jambhul showed retention of 30.83 % TPC, 10.40 % TFC, 9.31 %, TMAC, 12.75 % ascorbic acid, 19.26 % ABTS activity, 98.71 % DPPH activity, and 27.78 % FRAP activitys in IR drying; whereas wood apple showed more retention of 25.74 % TPC, 61 % ascorbic acid, 10.31 % ABTS, 36.45 % DPPH and 0.27 % FRAP in tray drying (TD). During storage bioactive constituents in jambhul powder were preserved at refrigeration temperatures whereas in wood apple they were retained at room temperature.

An actinomycete wild strain PM0626271 (= MTCC 5447), producing novel antibacterial compounds, was isolated from soil collected from Antarctica. The taxonomic status of the isolate was established by polyphasic approach. Scanning electron microscopy observations and the presence of LL-Diaminopimelic acid in the cell wall hydrolysate confirmed the genus Streptomyces. Analysis of 16S rRNA gene sequence showed highest sequence similarity to Streptomyces radiopugnans (99%). The phylogenetic tree constructed using near complete 16S rRNA gene sequences of the isolate and closely related strains revealed that although the isolate fell within the S. radiopugnans gene subclade, it was allocated a different branch in the phylogenetic tree, separating it from the majority of the radiopugnans strains. Similar to type strain, S. radiopugnans R97(T) , the Antarctica isolate displayed thermo tolerance as well as resistance to (60) Co gamma radiation, up to the dose of 15 kGy. However, media and salt tolerance studies revealed that, unlike the type strain, this isolate needed higher salinity for its growth. This is the first report of S. radiopugnans isolated from the Antarctica region. The GenBank/EMBL/DDBJ accession number for the 16S rRNA gene sequence of Streptomyces radiopugnans MTCC 5447 is JQ723477., (© 2013 Piramal Enterprises Ltd. Letters in Applied Microbiology © 2013 The Society for Applied Microbiology.)