ArticleMolecules (Basel, Switzerland)2019
Spectroscopic Technique-Based Comparative Investigation on the Interaction of Theaflavins with Native and Glycated Human Serum Albumin.
Article in Molecules (Basel, Switzerland), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 23 citations in OpenAlex.
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- The Structure of Zinc Chelidonate in the Crystalline Phase, Aqueous Solution and Assessment of the Interaction with Serum Albumin.Molecules (Basel, Switzerland) · 2026Article
- Unveiling the anti-glycation properties of acetylsalicylic acid: targeted inhibition of albumin glycation.Amino acids · 2026Article
- Bioavailability of Tea Polyphenols: A Key Factor in Understanding Their Mechanisms of Action In Vivo and Health Effects.Journal of agricultural and food chemistry · 2025Review
- Structural and in vitro anticancer properties of the kaempferol-lactoferrin complex.Food science & nutrition · 2024Article
- Probing the Interaction between Isoflucypram Fungicides and Human Serum Albumin: Multiple Spectroscopic and Molecular Modeling Investigations.International journal of molecular sciences · 2023Article
- Study on the Interaction Mechanism of Theaflavin with Whey Protein: Multi-Spectroscopy Analysis and Molecular Docking.Foods (Basel, Switzerland) · 2023Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Theaflavin is a kind of multi-pharmacological and health beneficial black tea factor. The aim of this study is to investigate the mechanisms by which theaflavin interacts with glycosylated and non-glycosylated serum albumins and compares their binding properties. Fluorescence and ultraviolet spectra indicated that theaflavin interacted with native and glycated human serum albumin through a static quenching mechanism and had a higher degree of quenching of human serum albumin. The thermodynamic parameters revealed that the combinations of theaflavin with native and glycated human serum albumin were a spontaneous endothermic reaction, and the hydrophobic force was a major driving force in the interaction process. Zeta potential, particle size, synchronous fluorescence, three-dimensional fluorescence spectroscopy and circular dichroism further clarified the effect of theaflavin on the conformation of human serum albumin structure were more pronounced. In addition, site competition experiments and molecular docking technique confirmed that the binding sites of theaflavin on both native and glycated human serum albumin were bound at site II. This study had investigated the effects of glycation on the binding of HSA with polyphenols and the potential nutriology significance of these effects.
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