Alpha-Casein as a Molecular Chaperone

Treweek, Teresa M.

doi:10.5772/48348

Cited by 9 publications

(25 citation statements)

References 152 publications

(267 reference statements)

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“…The phosphoserine residues occur in clusters on specific serine residues (SER) specified as phosphoseryle clusters, which aids in creating a flexible, amphiphilic, hydrophobic and hydrophilic structure. Both α caseins have molecular chaperon characteristics, that prevents coagulation and precipitation as a result of heat by stabilising its unfolded targeted proteins through interaction [39].…”

Section: Casein Micelles and Its Structurementioning

confidence: 99%

Casein Micelles as an Emerging Delivery System for Bioactive Food Components

Sadiq

Gill

Chandrapala

2021

Foods

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Bioactive food components have potential health benefits but are highly susceptible for degradation under adverse conditions such as light, pH, temperature and oxygen. Furthermore, they are known to have poor solubilities, low stabilities and low bioavailabilities in the gastrointestinal tract. Hence, technologies that can retain, protect and enable their targeted delivery are significant to the food industry. Amongst these, microencapsulation of bioactives has emerged as a promising technology. The present review evaluates the potential use of casein micelles (CMs) as a bioactive delivery system. The review discusses in depth how physicochemical and techno-functional properties of CMs can be modified by secondary processing parameters in making them a choice for the delivery of food bioactives in functional foods. CMs are an assembly of four types of caseins, (αs1, αs2, β and κ casein) with calcium phosphate. They possess hydrophobic and hydrophilic properties that make them ideal for encapsulation of food bioactives. In addition, CMs have a self-assembling nature to incorporate bioactives, remarkable surface activity to stabilise emulsions and the ability to bind hydrophobic components when heated. Moreover, CMs can act as natural hydrogels to encapsulate minerals, bind with polymers to form nano capsules and possess pH swelling behaviour for targeted and controlled release of bioactives in the GI tract. Although numerous novel advancements of employing CMs as an effective delivery have been reported in recent years, more comprehensive studies are required to increase the understanding of how variation in structural properties of CMs be utilised to deliver bioactives with different physical, chemical and structural properties.

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Section: Casein Micelles and Its Structurementioning

confidence: 99%

Casein Micelles as an Emerging Delivery System for Bioactive Food Components

Sadiq

Gill

Chandrapala

2021

Foods

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“…Protein spots 2, 3 and 13 were identified as α s2 -CN ( Figure 1a; Table 2), which display molecular chaperone properties that protect a wide range of proteins from milk and nonmilk sources against aggregation and precipitation under stress conditions (e.g. heat, reduction) (Treweek, 2012). Prizant and Barash (2008) documented that the AAs Lys, His and Thr negatively affect S6K1 phosphorylation in bovine mammary epithelial cells.…”

Section: Caseinsmentioning

confidence: 99%

Effects of the processing methods of corn grain and soybean meal on milk protein expression profiles in dairy cows

Shen

Liu

2015

Animal

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A proteomic approach was used to investigate the effects of the processing method of corn grain and soybean meal on the milk protein expression profile in lactating dairy cows. A total of 12 multiparous Holstein dairy cows were used in a 4 × 4 Latin square design with a 2 × 2 factorial arrangement. The primary factors examined were corn (finely ground (FGC) v. steam-flaked (SFC)) and soybean meal (solvent-extracted (SSBM) v. heat-treated (HSBM)), which were used to formulate four diets with the same basal ingredient: 27% FGC and 9% SSBM; 27% SFC and 9% SSBM; 27% FGC and 9% HSBM; and 27% SFC and 9% HSBM. Each period lasted for 21 days. Milk samples were collected on days 18, 19 and 20 of each period. Changes in the milk proteins were assessed by two-dimensional (2D) electrophoresis and ImageMaster 2D Platinum 6.0 software. A total of 13 spots displayed variations in protein spot abundance according to the statistical analysis. These spots were identified by a matrix-assisted laser desorption/ ionization-time of flight/time of flight MS. According to the gels, the relative abundance of α s2 -casein (CN) fragments was higher in the cows fed the SFC-HSBM than that for SFC-SSBM, whereas β-CN, α-lactalbumin and zinc-alpha-2-glycoprotein fragments were down-regulated in HSBM-fed cows. The relative decrease of β-CN expression was validated by western blot and agreed with the MS data. These results suggested that the method used to process soybean meal modified the synthesis and secretion of milk proteins in lactating dairy cows' mammary glands.

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“…In fact, amyloid formation, further than being involved in many diseases, may also represent a limit in protein purification, production, and storage. Among the inhibitors, milk casein proteins have been found to exert a chaperone-like activity against aggregation. − In particular, α S1 -casein (α-cas) is able to strongly retard the fibrillogenesis of 1–40 amyloid β-peptide (Aβ1–40), directly involved in Alzheimer’s disease, even at substoichiometric concentration …”

mentioning

confidence: 99%

“…Finally, because insulin is universally used as a drug in diabetes treatment and fibril formation may negatively affect its purification and production, ,, we think it is most important to explore new strategies to prevent its aggregation. Previous studies on the chaperone-like activity of caseins on insulin (amorphous) aggregation have been performed at neutral pH and under reductive stress, reporting a moderate effect. − Our experiments have been performed at pH 1.6 (see the Supporting Information), under conditions in which insulin is mainly dimeric …”

mentioning

confidence: 99%

α-Casein Inhibits Insulin Amyloid Formation by Preventing the Onset of Secondary Nucleation Processes

Librizzi

Carrotta

Spigolon

et al. 2014

J. Phys. Chem. Lett.

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α-Casein is known to inhibit the aggregation of several proteins, including the amyloid β-peptide, by mechanisms that are not yet completely clear. We studied its effects on insulin, a system extensively used to investigate the properties of amyloids, many of which are common to all proteins and peptides. In particular, as for other proteins, insulin aggregation is affected by secondary nucleation pathways. We found that α-casein strongly delays insulin amyloid formation, even at extremely low doses, when the aggregation process is characterized by secondary nucleation. At difference, it has a vanishing inhibitory effect on the initial oligomer formation, which is observed at high concentration and does not involve any secondary nucleation pathway. These results indicate that an efficient inhibition of amyloid formation can be achieved by chaperone-like systems, by sequestering the early aggregates, before they can trigger the exponential proliferation brought about by secondary nucleation mechanisms.

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Alpha-Casein as a Molecular Chaperone

Cited by 9 publications

References 152 publications

Casein Micelles as an Emerging Delivery System for Bioactive Food Components

Casein Micelles as an Emerging Delivery System for Bioactive Food Components

Effects of the processing methods of corn grain and soybean meal on milk protein expression profiles in dairy cows

α-Casein Inhibits Insulin Amyloid Formation by Preventing the Onset of Secondary Nucleation Processes

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