ArticleMolecules (Basel, Switzerland)2021
A Study of the Interaction, Morphology, and Structure in Trypsin-Epigallocatechin-3-Gallate Complexes.
Article in Molecules (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 15 citations in OpenAlex.
- Biophysical characterization and in silico analysis of natural and synthetic compounds targeting Listeria monocytogenes HtrA protease.Molecular diversity · 2025Article
- Composites of Pea Protein Nanofibril and Epigallocatechin Gallate: Formation Mechanism, Structural Characterization, and Antioxidant Activity.Foods (Basel, Switzerland) · 2025Article
- An Alternative Mechanism of Glutamate Dehydrogenase Inhibition by EGCG: Promotion of Protein Degradation.Pharmaceuticals (Basel, Switzerland) · 2025Article
- Food Antioxidants and Their Interaction with Human Proteins.Antioxidants (Basel, Switzerland) · 2023Review
- Key Enzymes in Fatty Acid Synthesis Pathway for Bioactive Lipids Biosynthesis.Frontiers in nutrition · 2022Review
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
Understanding the interaction between proteins and polyphenols is of significance to food industries. The aim of this research was to investigate the mode of aggregation for trypsin-EGCG (Epigallocatechin-3-gallate) complexes. For this, the complex was characterized by fluorescence spectroscopy, circular dichroism (CD) spectra, small-angel X-ray scattering (SAXS), and atomic force microscope (AFM) techniques. The results showed that the fluorescence intensity of trypsin-EGCG complexes decreased with increasing the concentration of EGCG, indicating that the interaction between trypsin and EGCG resulted in changes in the microenvironment around fluorescent amino acid residues. The results of CD analysis showed conformational changes in trypsin after binding with EGCG. The results from SAXS analysis showed that the addition of EGCG results in the formation of aggregates of trypsin-EGCG complexes, and increasing the concentration of EGCG resulted in larger aggregates. AFM images showed that the trypsin-EGCG complex formed aggregates of irregular ellipsoidal shapes with the size of about 200 × 400 × 200 nm, with EGCG interconnecting the trypsin particles. Overall, according to these results, it was concluded that the large aggregates of trypsin-EGCG complexes are formed from several small aggregates that are interconnected. The results of this study shed some light on the interaction between digestive enzymes and EGCG.
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