Food Hydrocolloids, Год журнала: 2025, Номер unknown, С. 111424 - 111424
Опубликована: Апрель 1, 2025
Язык: Английский
ChemSusChem, Год журнала: 2022, Номер 15(17)
Опубликована: Июль 21, 2022
Mechanochemical transformations have made chemists enter unknown territories, forcing a different chemistry perspective. While questioning or revisiting familiar concepts belonging to solution chemistry, mechanochemistry has broken new ground, especially in the panorama of organic synthesis. Not only does it foster "thinking outside box", but also opened reaction paths, allowing overcome weaknesses traditional exactly where use well-established solution-based methodologies rules out progress. In this Review, reader is introduced an intriguing research subject not yet fully explored and waiting for improved understanding. Indeed, study mainly focused on that, although impossible solution, become possible under mechanochemical processing conditions, simultaneously entailing innovation expanding chemical space.
Язык: Английский
Процитировано
193
Chemical Society Reviews, Год журнала: 2024, Номер 53(3), С. 1514 - 1551
Опубликована: Янв. 1, 2024
Assembly strategy and application direction of protein-based bioactive coatings.
Язык: Английский
Процитировано
27
Food Hydrocolloids, Год журнала: 2022, Номер 137, С. 108307 - 108307
Опубликована: Ноя. 16, 2022
Amyloid fibrils from plant-based food protein sources bear a large unexploited potential for applications in and other biomaterials due to their techno-functional features. However, low solubility highly complex, inhomogeneous composition often hamper fibrillization. The objective of this study was evaluate the feasibility amyloid fibril production hemp seed protein, known as sustainable low-allergenic source. Hemp concentrate (HPC), primarily constituted 11 S globulin edestin, with 89.0% (0.25% w/w HPC, pH 2) extracted using gentle micellization. Fibrillization HPC (2% w/w, 2, 90 °C, 300 rpm) monitored over 5 h by ThT fluorescence, exhibiting steep increase fluorescence signal after lag phase 180 min. SDS-PAGE analysis indicated progressive polypeptide hydrolysis upon heating formation proteinaceous aggregates 160 Conformational changes towards increased β-sheet content were demonstrated CD FTIR. morphology formed fibrillar characterized TEM AFM. While essentially linear, branching effects became visible kept increasing incubation time. After relatively short time 4 h, had an average height 7.8 nm, contour length 1.8 μm, persistence ∼2.7 μm. These results suggest, that under chosen conditions extraction incubation, forms flexible high aspect ratio tendency form branches. By revealing proteins formation, these contribute expand understanding plant
Язык: Английский
Процитировано
54
Scientific Reports, Год журнала: 2023, Номер 13(1)
Опубликована: Янв. 31, 2023
The deposition of proteins in the form amyloid fibrils is closely associated with several serious diseases. events that trigger conversion from soluble functional into insoluble are not fully understood. Many disease can similar structural characteristics as disease-associated fibrils, which highlights potential risk cross-seeding by amyloid-like structures encountered our surrounding. Of particular interest common food be transformed under conditions to cooking. We here investigate amyloid-β (Aβ), a peptide known during development Alzheimer's disease, 16 types derived or peptides. Kinetic studies using thioflavin T fluorescence output show none investigated protein accelerates aggregation Aβ. In at least two cases (hen egg lysozyme and oat isolate) we observe retardation aggregation, appears originate interactions between seeds Aβ aggregated form. results support view food-derived factor for pathology disease.
Язык: Английский
Процитировано
24
Food Hydrocolloids, Год журнала: 2023, Номер 149, С. 109587 - 109587
Опубликована: Ноя. 23, 2023
Язык: Английский
Процитировано
21
Langmuir, Год журнала: 2025, Номер unknown
Опубликована: Янв. 2, 2025
It is crucial to comprehend protein misfolding and aggregation in the domains of biomedicine, pharmaceuticals, proteins. Amyloid fibrils are formed when proteins misfold assemble, resulting debilitating illness known as "amyloidosis". This work investigates lysozyme fibrillation with pluronics (F68 F127). The effect on has been studied mechanistically using a combination calorimetric spectroscopic techniques. TEM images ThT binding experiment were used analyze conformation fibrils, results showed that accelerated process. When interact at different stages fibrillation, their pre- postmicellar concentrations show decrease Δ
Язык: Английский
Процитировано
1
Food Hydrocolloids, Год журнала: 2025, Номер unknown, С. 111233 - 111233
Опубликована: Фев. 1, 2025
Язык: Английский
Процитировано
1
Food Hydrocolloids, Год журнала: 2025, Номер unknown, С. 111254 - 111254
Опубликована: Фев. 1, 2025
Язык: Английский
Процитировано
1
International Journal of Biological Macromolecules, Год журнала: 2022, Номер 213, С. 1098 - 1114
Опубликована: Июнь 8, 2022
Язык: Английский
Процитировано
25
Nature Communications, Год журнала: 2023, Номер 14(1)
Опубликована: Март 2, 2023
β2-microglobulin (β2m) and its truncated variant ΔΝ6 are co-deposited in amyloid fibrils the joints, causing disorder dialysis-related amyloidosis (DRA). Point mutations of β2m result diseases with distinct pathologies. β2m-D76N causes a rare systemic protein deposited viscera absence renal failure, whilst β2m-V27M is associated deposits forming predominantly tongue. Here we use cryoEM to determine structures formed from these variants under identical conditions vitro. We show that each fibril sample polymorphic, diversity arising 'lego-like' assembly common building block. These results suggest 'many sequences, one fold' paradigm contrast recently reported 'one sequence, many folds' behaviour intrinsically disordered proteins such as tau Aβ.
Язык: Английский
Процитировано
17