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1.
Front Psychol ; 14: 1288774, 2023.
Article in English | MEDLINE | ID: mdl-38274677

ABSTRACT

Objective: Several studies in the specialized literature have reported that events such as the death of a loved one, job loss, divorce, illness, or retirement lead to an increase in the level of stress felt, and subsequently stress affects the person on several levels of life, such as: personal, relational, social, academic and at the same time sanogenic. The present paper explored the relationship between critical life events and psycho-emotional health among youths and the manner in which this relationship is mediated by the level of life satisfaction. Methods: The data was extracted using a sample of participants (between 20 and 40 years old) from several cities in Romania, who experienced one or more critical life events during the last year. Data organization and hypothesis testing were performed using IBM SPSS 23 and jamovi programs. For this purpose we used the simple regression analysis, Pearson correlation and mediation analysis. The scales used to conduct the research were: RS-14, SRRS, ERQ, CERQ, DASS-21 and SWLS. Results: The final sample of the study totaled 190 female and male Romanian participants aged between 20 and 40 (M = 24.45, SD = 5.27) who had experienced critical events during the last year, leading to psycho-emotional destabilization and a significantly lower level of life satisfaction. The prevalence of critical life events among these participants varied from one to five events (55.26%) and up to more than 16 critical events in the past year (2.63%). The presence of these events led to increased levels of stress, anxiety, or depression among participants. Furthermore, it appears that the presence of a high number of critical life events led to a decreased life satisfaction among participants, along with a greater tendency toward catastrophizing. Conclusion: Critical life events are increasingly frequent events in everyday life, and youth seems to be the period with the most changes. The research findings add to current findings about the practical implications that critical life events have on psycho-emotional health among youths. Therefore it appears to be a close relationship between critical life events, psycho-emotional health, and emotional regulation. At the same time, it seems that coping mechanisms have a central role in the level of life satisfaction among youths.

2.
Antioxidants (Basel) ; 11(10)2022 Oct 14.
Article in English | MEDLINE | ID: mdl-36290751

ABSTRACT

Emerging customized designs to upgrade the functional potential of freeze-dried apple pomace was used in this study, in order to transform the industrial by-products into ingredients containing probiotics, for a better and healthier food composition. The freeze-dried apple pomace was analyzed for free and bounded phenolic contents, highlighting a significant level of caffeic acid (4978.00 ± 900.00 mg/100 g dry matter (DM)), trans-cinnamic acid (2144.20 ± 37.60 mg/100 g DM) and quercetin 3-ß-D-glucoside (236.60 ± 3.12 mg/100 g DM). The pectin extraction yield was approximatively 24%, with a degree of esterification of 37.68 ± 1.74%, and a methoxyl content of 5.58 ± 0.88%. The freeze-dried apple pomace was added in a different ratio as a supplement to cultural medium of Loigolactobacillus bifermentans MIUG BL 16, suggesting a significant prebiotic effect (p < 0.05) at concentration between 1% and 2%. The apple pomace was used to design three freeze-dried ingredients containing probiotic, with a high level of polyphenolic content (6.38 ± 0.14 mg gallic acid equivalents/g DM) and antioxidant activity (42.25 ± 4.58 mMol Trolox/g DM) for the powder containing apple pomace ethanolic extract. When inulin was used as a prebiotic adjuvant, the obtained powder showed a 6 log/g DM viable cell count. The ingredients were added to fermented vegetable soy milk-based products, allowing us to improve the polyphenolic content, antioxidant activity and viable cell counts. The approach designed in this study allowed us to obtain ingredients suitable to add value to food, whereas premises to align with the current circular economy premises, by reintegrating the industrial waste as sources of high added value compounds, are also provided.

3.
J Am Soc Mass Spectrom ; 25(8): 1472-81, 2014 Aug.
Article in English | MEDLINE | ID: mdl-24845351

ABSTRACT

Bioaffinity analysis using a variety of biosensors has become an established tool for detection and quantification of biomolecular interactions. Biosensors, however, are generally limited by the lack of chemical structure information of affinity-bound ligands. On-line bioaffinity-mass spectrometry using a surface-acoustic wave biosensor (SAW-MS) is a new combination providing the simultaneous affinity detection, quantification, and mass spectrometric structural characterization of ligands. We describe here an on-line SAW-MS combination for direct identification and affinity determination, using a new interface for MS of the affinity-isolated ligand eluate. Key element of the SAW-MS combination is a microfluidic interface that integrates affinity-isolation on a gold chip, in-situ sample concentration, and desalting with a microcolumn for MS of the ligand eluate from the biosensor. Suitable MS-acquisition software has been developed that provides coupling of the SAW-MS interface to a Bruker Daltonics ion trap-MS, FTICR-MS, and Waters Synapt-QTOF- MS systems. Applications are presented for mass spectrometric identifications and affinity (K(D)) determinations of the neurodegenerative polypeptides, ß-amyloid (Aß), and pathophysiological and physiological synucleins (α- and ß-synucleins), two key polypeptide systems for Alzheimer's disease and Parkinson's disease, respectively. Moreover, first in vivo applications of αSyn polypeptides from brain homogenate show the feasibility of on-line affinity-MS to the direct analysis of biological material. These results demonstrate on-line SAW-bioaffinity-MS as a powerful tool for structural and quantitative analysis of biopolymer interactions.


Subject(s)
Amyloid beta-Peptides/analysis , alpha-Synuclein/analysis , Amino Acid Sequence , Amino Acid Substitution , Amyloid beta-Peptides/chemistry , Amyloid beta-Peptides/radiation effects , Animals , Antibodies, Monoclonal/metabolism , Antibody Affinity , Biosensing Techniques , Brain/metabolism , Cyclotrons , Epitopes , Feasibility Studies , Fourier Analysis , Humans , Mass Spectrometry , Mice, Transgenic , Microfluidic Analytical Techniques , Molecular Weight , Mutant Proteins/analysis , Mutant Proteins/chemistry , Mutant Proteins/radiation effects , Neurons/chemistry , Recombinant Proteins/analysis , Recombinant Proteins/chemistry , Recombinant Proteins/radiation effects , Sound , alpha-Synuclein/chemistry , alpha-Synuclein/genetics , alpha-Synuclein/radiation effects
4.
Methods Mol Biol ; 896: 399-412, 2012.
Article in English | MEDLINE | ID: mdl-22821540

ABSTRACT

Protein amyloidogenesis is generally considered to be a major cause of two most severe neurodegenerative disorders, Parkinson's disease (PD) and Alzheimer's disease (AD). Formation and accumulation of fibrillar aggregates and plaques derived from α-synuclein (α-Syn) and ß-amyloid (Aß) polypeptide in brain have been recognized as characteristics of Parkinson's disease and Alzheimer's disease. Oligomeric aggregates of α-Syn and Aß are considered as neurotoxic intermediate products leading to progressive neurodegeneration. However, molecular details of the oligomerization and aggregation pathway(s) and the molecular structure details are still unclear. We describe here the application of ion-mobility mass spectrometry (IMS-MS) to the identification of α-Syn and Aß oligomerization-aggregation products, and to the characterization of different conformational forms. IMS-MS is an analytical technique capable of separating gaseous ions based on their size, shape, and topography. IMS-MS studies of soluble α-Syn and Aß-aggregates prepared by in vitro incubation over several days were performed on a quadrupole time of flight mass spectrometer equipped with a "travelling wave" ion mobility cell, and revealed the presence of different conformational states and, remarkably, truncation and proteolytic products of high aggregating reactivity. These results suggest that different polypeptide sequences may contribute to the formation of oligomeric aggregates of heterogeneous composition and distinct biochemical properties.


Subject(s)
Amyloid beta-Peptides/chemistry , Mass Spectrometry/methods , Peptide Fragments/chemistry , Protein Multimerization , alpha-Synuclein/chemistry , Amino Acid Sequence , Molecular Sequence Data , Protein Structure, Secondary
5.
Chembiochem ; 12(18): 2740-4, 2011 Dec 16.
Article in English | MEDLINE | ID: mdl-22162214

ABSTRACT

Gas-phase protein separation by ion mobility: With its ability to separate the Parkinson's disease protein α-synuclein and its autoproteolytic products-despite the small concentrations of the latter-ion-mobility MS has enabled the characterization of intermediate fragments in in vitro oligomerization-aggregation. In particular, a possible key fragment, the highly aggregating C-terminal fragment, αSyn(72-140), has been revealed.


Subject(s)
Biopolymers/metabolism , Mass Spectrometry/methods , Parkinson Disease/metabolism , alpha-Synuclein/metabolism , Chromatography, High Pressure Liquid , Electrophoresis, Polyacrylamide Gel , Humans , Proteolysis , Spectrometry, Mass, Electrospray Ionization , Tandem Mass Spectrometry
6.
J Am Soc Mass Spectrom ; 21(10): 1643-8, 2010 Oct.
Article in English | MEDLINE | ID: mdl-20692851

ABSTRACT

We describe here an on-line combination of a surface acoustic wave (SAW) biosensor with electrospray ionization mass spectrometry (SAW-ESI-MS) that enables the direct detection, identification, and quantification of affinity-bound ligands from a protein-ligand complex on a biosensor chip. A trapping column was used between the SAW-biosensor and the electrospray mass spectrometer equipped with a micro-guard column, which provides simultaneous sample concentration and desalting for the mass spectrometric analysis of the dissociated ligand. First applications of the on-line SAW-ESI-MS combination include (1), differentiation of ß-amyloid (Aß) epitope peptides bound to anti-Aß antibodies; (2), the identification of immobilized Substance P peptide-calmodulin complex; (3), identification and quantification of the interaction of 3-nitrotyrosine-modified peptides with nitrotyrosine-specific antibodies; and (4), identification of immobilized anti-α-synuclein-human α-synuclein complex. Quantitative determinations of protein-ligand complexes by SAW yielded dissociation constants (K(D)) from micro-to low nanomolar sample concentrations. The on-line bioaffinity-ESI-MS combination presented here is expected to enable broad bioanalytical application to the simultaneous, label-free determination and quantification of biopolymer-ligand interactions, as diverse as antigen-antibody and lectin-carbohydrate complexes.


Subject(s)
Antibodies, Immobilized/metabolism , Biosensing Techniques/methods , Protein Interaction Mapping/methods , Proteins/metabolism , Spectrometry, Mass, Electrospray Ionization/methods , Amino Acid Sequence , Antibodies, Immobilized/chemistry , Antibodies, Monoclonal/chemistry , Antibodies, Monoclonal/metabolism , Humans , Lectins , Microchip Analytical Procedures , Protein Binding , Proteins/chemistry , Tyrosine/analogs & derivatives , Tyrosine/chemistry , Tyrosine/metabolism
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