ArticlePharmacological reports : PR2022
Comparative study of the binding between chlorogenic acid and four proteins by isothermal titration calorimetry, spectroscopy and docking methods.
Article in Pharmacological reports : PR, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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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.
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Who cites it
2 citing papers in PubMed, 8 citations in OpenAlex.
- Novel Insights into Milk Coffee Products: Component Interactions, Innovative Processing, and Healthier Product Features.Foods (Basel, Switzerland) · 2025Review
- Physicochemical Properties, Stability, and Functionality of Non-Covalent Ternary Complexes Fabricated with Pea Protein, Hyaluronic Acid and Chlorogenic Acid.Foods (Basel, Switzerland) · 2024Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
As a polyphenolic compound, chlorogenic acid has antioxidant, anti-inflammatory, antiviral, anti-obesity and other effects. Based on the interactions between chlorogenic acid and the proteins (human serum albumin (HSA), pepsin (Pep), trypsin (Try), fat mass and obesity-associated protein (FTO)), results will provide clues for screening effective inhibitors. The interaction between chlorogenic acid and the four proteins (HSA, Pep, Try, FTO) was analyzed by the aid of fluorescence quenching, synchronous fluorescence, three-dimensional fluorescence, isothermal titration calorimetry, and molecular docking. It can be concluded that there is no obvious interaction between chlorogenic acid and FTO. The binding affinity between chlorogenic acid and three proteins is HSA > Try > Pep. The binding process is spontaneous, and the quenching type is static quenching. Hydrophobic interaction and hydrogen bonding is observed in the binding process. This study provides valuable information for understanding the interaction mechanism between chlorogenic acid and proteins, and provides clues for screening inhibitors.
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