A Study of the Interaction, Morphology, and Structure in Trypsin-Epigallocatechin-3-Gallate Complexes

Overview

Journal Molecules

Publisher MDPI

Specialty Biology

Date 2021 Aug 7

PMID 34361715

Citations 3

Authors

Jiayin Liu

Hossein Ghanizadeh

Xinmao Li

Zhengyuan Han

Youwen Qiu

Yao Zhang

Xiuling Chen

Aoxue Wang

Affiliations

Soon will be listed here.

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.

Citing Articles

Biophysical characterization and in silico analysis of natural and synthetic compounds targeting Listeria monocytogenes HtrA protease.

Amrutha M, Wessler S, Ponnuraj K Mol Divers. 2024; .

PMID: 39604603 DOI: 10.1007/s11030-024-11050-0.

Food Antioxidants and Their Interaction with Human Proteins.

Nedic O, Penezic A, Minic S, Radomirovic M, Nikolic M, Cirkovic Velickovic T Antioxidants (Basel). 2023; 12(4).

PMID: 37107190 PMC: 10135064. DOI: 10.3390/antiox12040815.

Key Enzymes in Fatty Acid Synthesis Pathway for Bioactive Lipids Biosynthesis.

Zhuang X, Zhang Y, Xiao A, Zhang A, Fang B Front Nutr. 2022; 9:851402.

PMID: 35284441 PMC: 8905437. DOI: 10.3389/fnut.2022.851402.

References

Li D, Zhu M, Xu C, Chen J, Ji B . The effect of Cu2+ or Fe3+ on the noncovalent binding of rutin with bovine serum albumin by spectroscopic analysis. Spectrochim Acta A Mol Biomol Spectrosc. 2010; 78(1):74-9. DOI: 10.1016/j.saa.2010.08.069. View

Piekarska B, Skowronek M, Rybarska J, Stopa B, Roterman I, Konieczny L . Congo red-stabilized intermediates in the lambda light chain transition from native to molten state. Biochimie. 1996; 78(3):183-9. DOI: 10.1016/0300-9084(96)89503-4. View

Trombley J, Loegel T, Danielson N, Hagerman A . Capillary electrophoresis methods for the determination of covalent polyphenol-protein complexes. Anal Bioanal Chem. 2011; 401(5):1523-9. DOI: 10.1007/s00216-011-4846-1. View

Manach C, Williamson G, Morand C, Scalbert A, Remesy C . Bioavailability and bioefficacy of polyphenols in humans. I. Review of 97 bioavailability studies. Am J Clin Nutr. 2005; 81(1 Suppl):230S-242S. DOI: 10.1093/ajcn/81.1.230S. View

Saracila M, Panaite T, Papuc C, Criste R . Heat Stress in Broiler Chickens and the Effect of Dietary Polyphenols, with Special Reference to Willow ( spp Bark Supplements-A Review. Antioxidants (Basel). 2021; 10(5). PMC: 8146860. DOI: 10.3390/antiox10050686. View

Nugala B, Namasi A, Emmadi P, Krishna P . Role of green tea as an antioxidant in periodontal disease: The Asian paradox. J Indian Soc Periodontol. 2012; 16(3):313-6. PMC: 3498696. DOI: 10.4103/0972-124X.100902. View

Ohara M, Ohyama Y . Delivery and application of dietary polyphenols to target organs, tissues and intracellular organelles. Curr Drug Metab. 2013; 15(1):37-47. DOI: 10.2174/1389200214666131210143407. View

Shi S, Zhang Y, Xiong X, Huang K, Chen X, Peng M . The influence of flavonoids on the binding of pantoprazole to bovine serum albumin by spectroscopic methods: with the viewpoint of food/drug interference. Food Chem. 2012; 135(3):1083-90. DOI: 10.1016/j.foodchem.2012.05.049. View

Kataoka M, Kuwajima K, Tokunaga F, Goto Y . Structural characterization of the molten globule of alpha-lactalbumin by solution X-ray scattering. Protein Sci. 1997; 6(2):422-30. PMC: 2143659. DOI: 10.1002/pro.5560060219. View

10.

Bandyopadhyay P, Ghosh A, Ghosh C . Recent developments on polyphenol–protein interactions: effects on tea and coffee taste, antioxidant properties and the digestive system. Food Funct. 2012; 3(6):592-605. DOI: 10.1039/c2fo00006g. View

11.

Chen X, Khajeh J, Ju J, Gupta Y, Stanley C, Do C . Phosphatidylinositol 4,5-bisphosphate clusters the cell adhesion molecule CD44 and assembles a specific CD44-Ezrin heterocomplex, as revealed by small angle neutron scattering. J Biol Chem. 2015; 290(10):6639-52. PMC: 4358296. DOI: 10.1074/jbc.M114.589523. View

12.

Turrini F, Donno D, Beccaro G, Pittaluga A, Grilli M, Zunin P . Bud-Derivatives, a Novel Source of Polyphenols and How Different Extraction Processes Affect Their Composition. Foods. 2020; 9(10). PMC: 7598208. DOI: 10.3390/foods9101343. View

13.

Shi C, Tang H, Xiao J, Cui F, Yang K, Li J . Small-Angle X-ray Scattering Study of Protein Complexes with Tea Polyphenols. J Agric Food Chem. 2017; 65(3):656-665. DOI: 10.1021/acs.jafc.6b04630. View

14.

Engel M, VandenAkker C, Schleeger M, Velikov K, Koenderink G, Bonn M . The polyphenol EGCG inhibits amyloid formation less efficiently at phospholipid interfaces than in bulk solution. J Am Chem Soc. 2012; 134(36):14781-8. DOI: 10.1021/ja3031664. View

15.

Doniach S . Changes in biomolecular conformation seen by small angle X-ray scattering. Chem Rev. 2001; 101(6):1763-78. DOI: 10.1021/cr990071k. View

16.

Behrens M, He Y, Oliveira C, Andersen G, Pedersen J, Nielsen K . Structural analysis of RNA helicases with small-angle X-ray scattering. Methods Enzymol. 2012; 511:191-212. DOI: 10.1016/B978-0-12-396546-2.00031-0. View

17.

Pascal C, Poncet-Legrand C, Imberty A, Gautier C, Sarni-Manchado P, Cheynier V . Interactions between a non glycosylated human proline-rich protein and flavan-3-ols are affected by protein concentration and polyphenol/protein ratio. J Agric Food Chem. 2007; 55(12):4895-901. DOI: 10.1021/jf0704108. View

18.

Zhang H, Wang Y, Zhou Q . Investigation of the interactions of quercetin and morin with trypsin. Luminescence. 2009; 24(5):355-62. DOI: 10.1002/bio.1121. View

19.

Brglez Mojzer E, Knez Hrncic M, Skerget M, Knez Z, Bren U . Polyphenols: Extraction Methods, Antioxidative Action, Bioavailability and Anticarcinogenic Effects. Molecules. 2016; 21(7). PMC: 6273793. DOI: 10.3390/molecules21070901. View

20.

Orzechowski A, Ostaszewski P, Jank M, Berwid S . Bioactive substances of plant origin in food--impact on genomics. Reprod Nutr Dev. 2003; 42(5):461-77. DOI: 10.1051/rnd:2002037. View