ArticleJournal of food science and technology2017
Characterization of molecular structures of theaflavins and the interactions with bovine serum albumin.
Article in Journal of food science and technology, 2017. 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.
- The Structure of Zinc Chelidonate in the Crystalline Phase, Aqueous Solution and Assessment of the Interaction with Serum Albumin.Molecules (Basel, Switzerland) · 2026Article
- Research on the Interaction Mechanism and Structural Changes in Human Serum Albumin with Hispidin Using Spectroscopy and Molecular Docking.Molecules (Basel, Switzerland) · 2024Article
- Effects of theaflavin-gallatePhytomedicine plus : international journal of phytotherapy and phytopharmacology · 2022Article
- Elucidation of molecular interactions of theaflavin monogallate with camel milk lactoferrin: detailed spectroscopic and dynamic simulation studies.RSC advances · 2021Article
- The Non-Covalent Interactions and In Vitro Radical Scavenging Activities of the Caseinate-Galangin and Caseinate-Genistein Complexes.Antioxidants (Basel, Switzerland) · 2019Article
- Spectroscopic Technique-Based Comparative Investigation on the Interaction of Theaflavins with Native and Glycated Human Serum Albumin.Molecules (Basel, Switzerland) · 2019Article
- Depicting the Non-Covalent Interaction of Whey Proteins with Galangin or Genistein Using the Multi-Spectroscopic Techniques and Molecular Docking.Foods (Basel, Switzerland) · 2019Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this study, theaflavins (TF1, TF2A, TF2B and TF3) were prepared from black tea and their interaction with bovine serum albumin (BSA) was explored by fluorescence and CD spectroscopy. The results showed that the structures of theaflavins exhibited significant effects on the binding/quenching process, and the binding affinity increased with the increase of molecular weight of theaflavins and the presence of galloyl moiety. The quenching effects showed a sequence as TF3 > TF2A > TF2B > TF1, demonstrating the important role of the galloyl moiety on the C-3 position of theaflavins. CD spectra indicated that TF3 in high concentration could change the skeleton structure of BSA and induce the unfolding of BSA secondary structure. The present results provide a new perspective for better understanding of the likely physiological fate of theaflavins and help to control the functional characteristics of food.
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