ArticleFoods (Basel, Switzerland)2023
Study on the Interaction Mechanism of Theaflavin with Whey Protein: Multi-Spectroscopy Analysis and Molecular Docking.
Article in Foods (Basel, Switzerland), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
4 citing papers in PubMed.
- Dual enhancement of pork color stability: Antioxidant activity and myoglobin structural compactness mediated by L-histidine/L-arginine.Food chemistry: X · 2025Article
- Enhancement of antioxidant and antimicrobial properties of Whey protein isolate and chlorogenic acid complexes through enzymatic and alkaline techniques.Scientific reports · 2025Article
- Whey protein isolate-reuterin complexes: Structure and functional properties.Food chemistry: X · 2025Article
- The Effect of Nanoscale Modification of Nisin by Different Milk-Derived Proteins on Its Physicochemical Properties and Antibacterial Activity.Foods (Basel, Switzerland) · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
The interaction mechanism of whey proteins with theaflavin (TF1) in black tea was analyzed using multi-spectroscopy analysis and molecular docking simulations. The influence of TF1 on the structure of bovine serum albumin (BSA), β-lactoglobulin (β-Lg), and α-lactoalbumin (α-La) was examined in this work using the interaction of TF1 with these proteins. Fluorescence and ultraviolet-visible (UV-vis) absorption spectroscopy revealed that TF1 could interact with BSA, β-Lg and α-La through a static quenching mechanism. Furthermore, circular dichroism (CD) experiments revealed that TF1 altered the secondary structure of BSA, β-Lg and α-La. Molecular docking demonstrated that the interaction of TF1 with BSA/β-Lg/α-La was dominated by hydrogen bonding and hydrophobic interaction. The binding energies were -10.1 kcal mol
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.