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Nutrients Jul 2023The number of individuals experiencing mental disorders (e.g., anxiety and depression) has significantly risen in recent years. Therefore, it is essential to seek... (Review)
Review
The number of individuals experiencing mental disorders (e.g., anxiety and depression) has significantly risen in recent years. Therefore, it is essential to seek prevention and treatment strategies for mental disorders. Several gut microbiota, especially Firmicutes and Bacteroidetes, are demonstrated to affect mental health through microbiota-gut-brain axis, and the gut microbiota dysbiosis can be related to mental disorders, such as anxiety, depression, and other mental disorders. On the other hand, dietary components, including probiotics (e.g., and ), prebiotics (e.g., dietary fiber and alpha-lactalbumin), synbiotics, postbiotics (e.g., short-chain fatty acids), dairy products, spices (e.g., , curcumin, and capsaicin), fruits, vegetables, medicinal herbs, and so on, could exert protective effects against mental disorders by enhancing beneficial gut microbiota while suppressing harmful ones. In this paper, the mental disorder-associated gut microbiota are summarized. In addition, the protective effects of dietary components on mental health through targeting the gut microbiota are discussed. This paper can be helpful to develop some dietary natural products into pharmaceuticals and functional foods to prevent and treat mental disorders.
Topics: Humans; Gastrointestinal Microbiome; Anxiety; Depression; Mental Disorders; Prebiotics; Probiotics; Synbiotics; Biological Products
PubMed: 37513676
DOI: 10.3390/nu15143258 -
Pharmacology, Biochemistry, and Behavior Jul 2024Milk varieties and specific proteins exhibit anxiolytic-like actions in mice and rats exposed to several tests, the most prominent being the elevated plus-maze.... (Review)
Review
Milk varieties and specific proteins exhibit anxiolytic-like actions in mice and rats exposed to several tests, the most prominent being the elevated plus-maze. Administrations of α-casein, its 91-100 (α-casozepine), 91-97, 91-93, and 91-92 fragments, the 60-69 fragment of β-casein, lactoferrin, β-lactotensin, wheylin-1, wheylin-2, and α-lactalbumin have been reported to increase open arm exploration relative to enclosed arm exploration. Anxiolytic-like actions have also been described for 91-93 and 91-92 fragments of α-casein, wheylin-1, α-lactalbumin, and lactoferrin in the open-field. Some effects appear to be mediated by the GABA receptor complex, since antagonists mitigated the anxiolytic-like actions of α-casein, the 91-92 fragment of α-casein, and wheylin-1. Other neurotransmitters purported to affect such behaviors include 5HT, dopamine, and neurotensin. Further research is needed to identify their neuropharmacological actions.
Topics: Animals; Anti-Anxiety Agents; Mice; Milk Proteins; Anxiety; Rats; Behavior, Animal; Humans; Caseins
PubMed: 38735399
DOI: 10.1016/j.pbb.2024.173789 -
Journal of Sleep Research Jan 2024Insufficient sleep is a growing global problem, with poor sleep associated with many negative health and performance outcomes. Previous reviews investigating the effect... (Review)
Review
Insufficient sleep is a growing global problem, with poor sleep associated with many negative health and performance outcomes. Previous reviews investigating the effect of diet on sleep have highlighted the amino acid tryptophan as a promising sleep-promoting nutrient, with the richest food source of tryptophan, ⍺-lactalbumin, requiring further investigation. Therefore, this systematic review aimed to review the existing evidence of association between ⍺-lactalbumin and sleep. Four electronic databases (CINAHL Complete, Embase, MEDLINE Complete, and SPORTDiscus with Full Text) were searched from database inception to March 2023, with primary research articles included if they contained α-lactalbumin as an independent variable, an outcome measure of sleep or sleepiness, and participants were ≥ 18 years old. Eight studies were reviewed, with four studies recruiting athletic populations (50%) and four recruiting healthy participants (50%). Sleep or sleepiness was measured objectively in six studies (75%), with two studies employing polysomnography and four utilizing actigraphy to assess sleep. Across the studies, 20-60 g of ⍺-lactalbumin was supplemented, with five studies (63%) observing a positive association between α-lactalbumin and sleep. Sleep-onset latency was the primary sleep metric improved following evening supplementation of α-lactalbumin (≤ 3.5 hr pre-sleep), with no studies observing any negative associations with sleep. Data from this review suggest that individuals that have difficulty initiating sleep may benefit most from pre-sleep α-lactalbumin supplementation. Further research is required to establish the effect that α-lactalbumin has on sleep architecture, through the use of more comprehensive sleep analysis tools such as portable electroencephalography or polysomnography, in combination with stringent dietary controls.
PubMed: 38185736
DOI: 10.1111/jsr.14141 -
Journal of Food Science Jul 2023Protein nanostructures can be used in food applications to improve the techno-functional properties of a food formulation. This study aims to find the best conditions...
Protein nanostructures can be used in food applications to improve the techno-functional properties of a food formulation. This study aims to find the best conditions for the production and conformational change of α-lactalbumin nanostructured aggregates. The criteria to determine the best operating conditions to produce α-lactalbumin nanostructured aggregates were intensification of foaming and emulsification, techno-functional proprieties, cytotoxic, and antibacterial activity of nanostructures compared with native α-lactalbumin. Conformational alterations occurred in the α-helix and sheet-β protein structures. The size obtained by dynamic light scattering was 163.84 nm with a polydispersity index of 0.29. The nano protein improved the techno-functional property compared to the native protein. Additionally, nanostructures had no cytotoxic effect and were innocuous to bacterial activity. Thus, this study presents the best conditions to produce α-lactalbumin nanostructured aggregates with improved properties that allow new food industry applications.
Topics: Lactalbumin; Nanostructures
PubMed: 37248720
DOI: 10.1111/1750-3841.16622 -
Foods (Basel, Switzerland) Jul 2023The characteristics and the functions of Maillard reaction products (MRPs) produced by polydextrose (PD), a new type of prebiotic, and α-lactalbumin (α-LA) were...
The characteristics and the functions of Maillard reaction products (MRPs) produced by polydextrose (PD), a new type of prebiotic, and α-lactalbumin (α-LA) were valued. PD and α-LA were incubated at 60 °C and 79% relative humidity for up to 72 h to prepare MRPs. The results showed that the absorbance and fluorescence intensity of heated α-LA-PD increased, and the amount of free amino groups reduced as the reaction progressed, which confirmed the formation of different stages of MRPs. Electrophoresis revealed an increase in molecular mass and the degree of covalent cross-linking. The secondary structure of MRPs experienced no significant changes with the measurement of circular dichroism (CD), while the tertiary structure gradually unfolded, exposing hydrophobic groups. Furthermore, a significant increase was detected in the radical-scavenging activity of 2,2-diphenyl-1-picrylhydrazyl (DPPH) and the ferric reducing/antioxidant power (FRAP) of MRPs. The findings offer a foundation for understanding the structural and functional features of MRPs in formula milk powder.
PubMed: 37569135
DOI: 10.3390/foods12152866 -
Spectrochimica Acta. Part A, Molecular... Nov 2023The combination of light and photoresponsive compounds provides a peculiar way of regulating biological systems. Azobenzene is a classical organic compound with...
The combination of light and photoresponsive compounds provides a peculiar way of regulating biological systems. Azobenzene is a classical organic compound with photoisomerization properties. Exploring the interactions between azobenzene and proteins can deepen the biochemical applications of the azobenzene compounds. In this paper, the interaction of 4-[(2,6-dimethylphenyl)diazenyl]-3,5-dimethylphenol with alpha-lactalbumin was investigated by UV-Vis absorption spectra, multiple fluorescence spectra, computer simulations, and circular dichroism spectra. Most critically, the interaction differences between proteins and the trans- and cis-isomer of ligands have been analyzed and compared. Results showed that both isomers of ligands were bound to alpha-lactalbumin to form ground state complexes and statically quenched the steady-state fluorescence of alpha-lactalbumin. The van der Waals forces and hydrogen bonding dominated the binding; the difference is that the binding of the cis-isomer to alpha-lactalbumin is more rapidly stabilized, and the binding strength is greater than the trans-isomer. These binding differences were modeled and analyzed by molecular docking and kinetic simulations, and we found that both isomers bind through the hydrophobic aromatic cluster 2 of alpha-lactalbumin. However, the bent structure of the cis-isomer is more closely aligned with the construction of the aromatic cluster and may have contributed to the above differences.
Topics: Lactalbumin; Molecular Docking Simulation; Ligands; Thermodynamics; Computer Simulation; Circular Dichroism
PubMed: 37327501
DOI: 10.1016/j.saa.2023.122965 -
Nutrients Jul 2023The primary control of dysmetabolic patients is extremely challenging worldwide, with inadequate dietary habits and sporadic physical activity among the key risk factors...
The primary control of dysmetabolic patients is extremely challenging worldwide, with inadequate dietary habits and sporadic physical activity among the key risk factors for metabolic syndrome onset. Nowadays, there is no exclusive treatment for this condition, and considering that preventive measures usually fail, new therapeutic approaches need to be proposed and investigated. This present pilot study compared the effects of diet alone and in association with a combination of myo-inositol and d-chiro-inositol in their 40:1 ratio, α-lactalbumin, and on different metabolic parameters in obese dysmetabolic patients. To this purpose, 37 patients with BMI between 30 and 40 and fasting blood glucose between 100 and 125 mg/dL were divided into two groups: () the control group followed a hypocaloric Mediterranean diet, () while the study group was also supplemented with a daily dosage of two sachets, each one containing 1950 mg myo-inositol, 50 mg d-chiro-inositol, 50 mg α-lactalbumin, and 250 mg . After a 6-month treatment, all parameters improved in both groups. Nevertheless, the treated group experienced a greater improvement, especially concerning the variation from the baseline of HOMA index, triglycerides, BMI, body weight, and waist circumference. These findings support the supplementation with myo-inositol and d-chiro-inositol in the 40:1 ratio, α-lactalbumin, and as a therapeutical strategy to potentiate the beneficial effects induced via dietary programs in dysmetabolic patients.
Topics: Humans; Female; Lactalbumin; Gymnema sylvestre; Inositol; Pilot Projects; Diet; Obesity; Body Weight; Metabolome; Polycystic Ovary Syndrome
PubMed: 37513560
DOI: 10.3390/nu15143142 -
Nano Letters Apr 2024Metal ions play a dual role in biological systems. Although they actively participate in vital life processes, they may contribute to protein aggregation and misfolding...
Metal ions play a dual role in biological systems. Although they actively participate in vital life processes, they may contribute to protein aggregation and misfolding and thus contribute to development of diseases and other pathologies. In nanofabrication, metal ions mediate the formation of nanostructures with diverse properties. Here, we investigated the self-assembly of α-lactalbumin into nanotubes induced by coordination with metal ions, screened among the series Mn, Co, Ni, Zn, Cd, and Au. Our results revealed that the affinity of metal ions toward hydrolyzed α-lactalbumin peptides not only impacts the kinetics of nanotube formation but also influences their length and rigidity. These findings expand our understanding of supramolecular assembly processes in protein-based materials and pave the way for designing novel materials such as metallogels in biochip and biosensor applications.
PubMed: 38598498
DOI: 10.1021/acs.nanolett.4c00601 -
Food Chemistry Dec 2023High internal phase Pickering emulsions (HIPPEs) stabilized by protein nanoparticles have been widely reported, but the use of enzymatic methods for preparing these...
High internal phase Pickering emulsions (HIPPEs) stabilized by protein nanoparticles have been widely reported, but the use of enzymatic methods for preparing these nanoparticles remains underexplored. Our hypothesis is that enzymatically crosslinked α-lactalbumin (ALA) nanoparticles (ALATGs) prepared using transglutaminase will demonstrate improved properties as stabilizers for HIPPEs. In this study, we investigated the physicochemical properties and microstructures of ALATGs, finding that enzymatic crosslinking could be enhanced by removing Ca ions from ALA and preheating the proteins (85 °C, 15 min). The electrical charge, secondary structure, and surface hydrophobicity of ALATGs were found to depend on crosslinking conditions. HIPPEs formed with an ALA concentration of 10 mg/mL and an enzyme activity of 120 U/g exhibited the highest apparent viscosity and mechanical strength, as well as significantly improved loading capacity and photostability for the encapsulated lycopene. Overall, our results support the hypothesis that ALATG-nanoparticles show superior performance as emulsifiers compared to ALA-nanoparticles.
Topics: Lactalbumin; Lycopene; Hydrophobic and Hydrophilic Interactions; Emulsions; Nanoparticles; Transcription Factors; Particle Size
PubMed: 37478605
DOI: 10.1016/j.foodchem.2023.136394 -
Biomacromolecules Sep 2023Proteins used as building blocks to template nanostructures with manifold morphologies have been widely reported. Understanding their self-assembly and reassembly...
Proteins used as building blocks to template nanostructures with manifold morphologies have been widely reported. Understanding their self-assembly and reassembly mechanism is important for designing functional biomaterials. Herein, we show that enzyme-hydrolyzed α-lactalbumin (α-lac) can self-assemble into either nanotubes in the presence of Ca ions or nanospheres in the absence of Ca in solution. Remarkably, such assembled α-lac nanotubes can be elongated by adding preassembled α-lac nanospheres and Ca solution, which suggests that the self-assembled α-lac nanospheres undergo disassembly and reassembly processes into existing nanotube nuclei. By performing atomic force microscopy (AFM), transmission electron microscopy (TEM), and confocal laser scanning microscopy (CLSM), it indicates that there is an equilibrium among nanotubes, nanospheres, hydrolyzed α-lac, and Ca in solution. The structural transition between nanotubes and nanospheres is driven from a less stable structure into a more stable structure determined by the conditions. During the transition from nanospheres into nanotubes, the hydrolyzed α-lac in nanospheres transfers into helical ribbon form at both nanotube extremities. Then helical ribbons close into mature nanotubes, extending the length of the initial nuclei. Besides, by dilution or adding ethylene glycol bis(2-aminoethyl ether) tetraacetic acid (EGTA), the decreased Ca concentration in solution drives the Ca dissociating from nanotubes into solution, leading to the transitions from nanotubes into nanospheres. The reversible transformation between nanotubes and nanospheres is achieved by adjusting the pH value from 7.5 to 5.0 and back to 7.5. This is because the stability of nanotubes decreases from pH 7.5 to 5 but increases from 5 to 7.5. Significantly, this approach can be used for the fabrication of various responsive nanomaterials from the same starting material.
Topics: Nanospheres; Ions; Nanotubes; Nanostructures; Biocompatible Materials
PubMed: 37642585
DOI: 10.1021/acs.biomac.3c00284