Probing the particle formation and aggregation behaviour of gliadin in aqueous ethanol with ultra-small- and small-angle X-ray scattering
Bibliographic record
Abstract
Colloidal gliadin particles show promise for use as interface stabilizers and for the encapsulation and delivery of bioactive molecules in food systems. Gliadin particles can be produced with a simple liquid anti-solvent precipitation (LAS) technique. The dynamics of the protein interactions and conformational changes due to changes in solvent quality during LAS have yet to be fully unravelled. In this study, ultra-small- and small-angle x-ray scattering (USAXS/SAXS) were used to investigate the assembly of gliadin proteins into particles and aggregates throughout LAS. Three regimes of gliadin assembly were identified at high (50−70 v/v%), intermediate (30−40 v/v%), and low (12−20 v/v%) ethanol concentrations. At high ethanol concentrations, primary structural units were identified in the high-q region (q > 2 × 10 -2 Å -1 ), believed to be gliadin molecules with coiled structures (R g1 = 6−7 nm, P 1 ≈ 2). At intermediate ethanol concentrations, polydisperse protein structures were formed. At low ethanol concentrations, two hierarchical structural levels were identified, with gliadin particles (R g2 ≈ 200–500 nm, 3.5 < P 2 < 4) identified at low-q (q < 2 × 10 -2 Å -1 ) believed to be formed by the assembly of primary structural units which had similar size and shape to those identified in high ethanol samples. Analysis with Fourier-transform infrared spectroscopy indicated that gliadin underwent secondary structural changes, with an increase in intermolecular β-sheets as the solvent quality was reduced during particle formation. This multi-scale investigation provides insight into the structural changes and interactions that occur during gliadin particle production with LAS. • The unified fit model was used to identify hierarchical gliadin structures in ethanol. • Polymer coil primary scattering units were identified at high ethanol concentrations. • Primary scattering units assembled into particles at low ethanol concentrations. • Intermolecular β-sheet structures increased when particles were formed.
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How this classification was reachedexpand
Full frame machine prediction
Teacher imitationNot calibrated prevalence, not ground truth. Human validation pending. The Gemma side is a direct model label for every work in the frame, read from the title-only record. The Codex side is a classifier learned from the 10,348 direct Codex labels and calibrated to design-weighted sample rates; fields without enough sample support carry no Codex call. Candidate is the union of the two sides; consensus is their intersection. These outputs are machine_predicted_unvalidated and are not human labels.
Distilled classifier scores by category (both heads)
| Category | Codex | Gemma |
|---|---|---|
| Metaresearch | 0.000 | 0.000 |
| Meta-epidemiology (narrow) | 0.000 | 0.000 |
| Meta-epidemiology (broad) | 0.000 | 0.000 |
| Bibliometrics | 0.000 | 0.000 |
| Science and technology studies | 0.000 | 0.000 |
| Scholarly communication | 0.000 | 0.000 |
| Open science | 0.000 | 0.000 |
| Research integrity | 0.000 | 0.000 |
| Insufficient payload (model declined to judge) | 0.000 | 0.000 |
Machine scores (provisional)
The two teacher heads of the student model, read on this work. A score orders the frame for review; it never asserts a category, and the validation status ships verbatim with every row.
Baseline scores from an immature model (maturity gate not passed, 7 training rounds). Scores rank; they never assert a category.
score_only:v0-immature-baseline · verbatim from the scoring run: score_only means the number may rank works, and no category label ships from itClassification
machine, unvalidatedMachine predicted; a candidate call from one source (direct Gemma or distilled Codex), not a consensus.
How this classification was reached, model by model and score by score, is at the end of the page under "How this classification was reached".