Authors:
,
,
,
, and
Y. Li
Y. Li
School of Medicine, Shenzhen University, Shenzhen, Guangdong Province, PR China
Search for other papers by Y. Li in
Current site
Google Scholar
PubMed
Search for other papers by Y. Li in
Current site
Google Scholar
PubMed
F.Q. Lu
F.Q. Lu
School of Medicine, Shenzhen University, Shenzhen, Guangdong Province, PR China
Search for other papers by F.Q. Lu in
Current site
Google Scholar
PubMed
Search for other papers by F.Q. Lu in
Current site
Google Scholar
PubMed
Y. Feng
Y. Feng
School of Medicine, Shenzhen University, Shenzhen, Guangdong Province, PR China
Search for other papers by Y. Feng in
Current site
Google Scholar
PubMed
Search for other papers by Y. Feng in
Current site
Google Scholar
PubMed
Z.D. He
Z.D. He
School of Medicine, Shenzhen University, Shenzhen, Guangdong Province, PR China
Search for other papers by Z.D. He in
Current site
Google Scholar
PubMed
Search for other papers by Z.D. He in
Current site
Google Scholar
PubMed
X.L. Wu
X.L. Wu
School of Medicine, Shenzhen University, Shenzhen, Guangdong Province, PR China
Search for other papers by X.L. Wu in
Current site
Google Scholar
PubMed
Search for other papers by X.L. Wu in
Current site
Google Scholar
PubMed
Analysis of the binding interaction of (−)-epigallocatechin-3-gallate (EGCG) and pepsin is important for understanding the inhibition of digestive enzymes by tea polyphenols. We studied the binding of EGCG to pepsin using fluorescence spectroscopy, Fourier transform infrared spectroscopy, isothermal titration calorimetry, and protein-ligand docking. We found that EGCG could inhibit pepsin activity. According to thermodynamic parameters, a negative ΔG indicated that the interaction between EGCG and pepsin was spontaneous, and the electrostatic force accompanied by hydrophobic binding forces may play major role in the binding. Data from multi-spectroscopy and docking studies suggest that EGCG could bind pepsin with a change in the native conformation of pepsin. Our results provide further understanding of the nature of the binding interactions between catechins and digestive enzymes.
ProCite
RefWorks
Reference Manager
BibTeX
Zotero
EndNote
-
BANDYOPADHYAY, P., GHOSH, A.K. & GHOSH, C. (2012): Recent developments on polyphenol–protein interactions: effects on tea and coffee taste, antioxidant properties and the digestive system. Food Funct., 3, 592–605.
-
BYLER, D.M. & SUSI, H. (1986): Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers, 25, 469–487.
-
DONG, A., HUANG, P. & CAUGHEY, W.S. (1990): Protein secondary structures in water from second-derivative amide I infrared spectra. Biochemistry, 29, 3303–3308.
-
DUBEAU, S., SAMSON, G. & TAJMIR-RIAHI, H.-A. (2010): Dual effect of milk on the antioxidant capacity of green, Darjeeling, and English breakfast teas. Food Chem., 122, 539–545.
-
HE, Q., LV, Y.P. & YAO, K. (2006): Effects of tea polyphenols on the activities of a-amylase, pepsin, trypsin and lipase. Food Chem., 101, 1178–1182.
-
JIANG, C.Q., GAO, M.X. & HE, J.X. (2002): Study of the interaction between terazosin and serum albumin: Synchronous fluorescence determination of terazosin. Anal. Chim. Acta, 452, 185–189.
-
KILMARTIN, P.A. & HSU, C.F. (2003): Characterisation of polyphenols in green, oolong, and black teas, and in coffee, using cyclic voltammetry. Food Chem., 82, 501–512.
-
LAKOWICZ, J R. (1999): Principles of fluorescence spectroscopy, 2nd ed., Kluwer Academic/Plenum Publishers, New York, NY. 725 pages.
-
LAKOWICZ, J.R. & WEBER, G. (1973): Quenching of protein fluorescence by oxygen. Detection of structural fluctuations in proteins on the nanosecond time scale. Biochemistry, 12, 4171–4179.
-
PRIGENT, S.V., GRUPPEN, H., VISSER, A.J., VAN KONINGSVELD, G.A., DE JONG, G.A. & VORAGEN, A.G. (2003): Effect of non-covalent interactions with 5-O-coffeoylquinic acid (chlorogenic acid) on the heat denaturation and solubility of globular p roteins. J. Agr. Food Chem., 51, 5088–5095.
-
ROSS, P.D. & SUBRAMANIAN, S. (1981): Thermodynamics of protein association reactions: Forces contributing to stability. Biochemistry, 20, 3096–3102.
-
SABU, M.C., PRIYA, T.T., RAMADASAN, K. & IKUO, N. (2010): Beneficial effects of green tea: A literature review. Chinese Medicine, 5, 13–22.
-
SIEBERT, K.J., TROUKHANOVA, N.V. & LYNN, P.Y. (1996): Nature of polyphenol-protein interactions. J. Agr. Food Chem., 44, 80–85.
-
SINKOVITS, A.F., BRYKSA, B.C., TANAKA, T. & YADA, R. Y. (2007): Understanding the structure-function role of specific catalytic residues in a model food related enzyme: pepsin. Enzyme Microb. Tech., 40, 1175–1180.
-
SPENCER, C.M., CAI, Y., MARTIN, R., GAFFNEY, S.H., GOULDING, P.N., MAGNOLATO, D., LILLEY, T.H., HASLAM, E. (1988): Polyphenol complexation – some thoughts and observations. Phytochemistry, 27, 2397–2409.
-
SUSI, H. & BYLER, D.M. (1986): Resolution-enhanced Fourier transform infrared spectroscopy of enzymes. Methods Enzymol., 130, 290–311.
-
TANTIPOLPHAN, R., RADES, T. & MEDLICOTT, N.J. (2007): Swelling lecithin: cholesterol implants for the controlled release of proteins. Int. J. Pharm., 337, 40–47.
-
WANG, C., WU, Q.H., WANG, Z. & ZHAO, J. (2006): Study of the interaction of carbamazepine with bovine serum albumin by fluorescence quenching method. Anal. Sci., 22, 435–438.
-
WU, X.L., WU, H., LIU, M.X., LIU, Z.H., XU, H. & LAI, F.R. (2011): Analysis of binding interaction between (-)-epigallocatechin (EGC) and β-lactoglobulin by multi-spectroscopic method. Spectrochim. Acta A., 82, 164–168.
-
WU, X.L., RAJE, D., WU, H., LIU, Z.G., HE, Q.Q. & ZENG, X.J. (2012): Studies on the interaction of EGCG with bovine β-lactoglobulin by spectroscopic methods and docking. Int. J. Dairy Technol., 65, 7–13.
-
WU, X.L., HE, W.Y., LI, Y., ZHANG, H.P., LIU, Z.G., WANG, W.P., YE. Y. & CAO, J.J. (2013): Characterization of binding interactions of (-)-epigallocatechin-3-gallate from green tea and lipase. J. Agr. Food Chem., 61, 8829–8835.
-
WU, X.L., HE, W.Y., ZHANG, H.P., LI, Y., LIU, Z.G. & HE, Z.D. (2014): Acteoside: A lipase inhibitor from the Chinese tea Ligustrum purpurascens kudingcha. Food Chem., 142, 306–310.
-
XIAO, J.B., SHI, J., CAO, H., WU, S.D., REN, F.L. & XU, M. (2007): Analysis of binding interaction between puerarin and bovine serum albumin by multi-spectroscopic method. J. Pharmaceut. Biomed., 45, 609–615.
-
XIE, M.X., XU, X.Y. & WANG, Y.D. (2005): Interaction between hesperetin and human serum albumin revealed by spectroscopic methods. BBA-Gen Subjects, 1724, 215–224.
-
YAN, Y., HU, J. & YAO, P. (2009): Effects of casein, ovalbumin, and dextran on the astringency of tea polyphenols determined by quartz crystal microbalance with dissipation. Langmuir, 25, 397–402.
-
YUKSEL, Z., AVCI, E. & EREEM., Y.K. (2010): Characterization of binding interactions between green tea flavanoids and milk proteins. Food Chem., 121, 450–456.
-
ZHU, R.R., WANG, W.R., SUN, X.Y, LIU, H. & WANG, S.L. (2010): Enzyme activity inhibition and secondary structure disruption of nano-TiO2 on pepsin. Toxicol. in Vitro., 24, 1639–1647.
Acta Alimentaria
E-mail: Acta.Alimentaria@uni-mate.hu
Indexing and Abstracting Services:
- Biological Abstracts
- BIOSIS Previews
- CAB Abstracts
- CABELLS Journalytics
- Chemical Abstracts
- Current Contents: Agriculture, Biology and Environmental Sciences
- Elsevier Science Navigator
- Essential Science Indicators
- Global Health
- Index Veterinarius
- Science Citation Index
- Science Citation Index Expanded (SciSearch)
- SCOPUS
- The ISI Alerting Services
| 2024 | |
|---|---|
| Scopus | |
| CiteScore | |
| CiteScore rank | |
| SNIP | |
| Scimago | |
| SJR index | 0.226 |
| SJR Q rank | Q3 |
| 2023 | |
|---|---|
| Web of Science | |
| Journal Impact Factor | 0,8 |
| Rank by Impact Factor | Q4 (Food Science & Technology) |
| Journal Citation Indicator | 0.19 |
| Scopus | |
| CiteScore | 1.8 |
| CiteScore rank | Q3 (Food Science) |
| SNIP | 0.323 |
| Scimago | |
| SJR index | 0.235 |
| SJR Q rank | Q3 |
| Acta Alimentaria | |
|---|---|
| Publication Model | Hybrid |
| Submission Fee | none |
| Article Processing Charge | 450 EUR/article (only for OA publications) |
| Printed Color Illustrations | 40 EUR (or 10 000 HUF) + VAT / piece |
| Regional discounts on country of the funding agency | World Bank Lower-middle-income economies: 50% World Bank Low-income economies: 100% |
| Further Discounts | Editorial Board / Advisory Board members: 50% Corresponding authors, affiliated to an EISZ member institution subscribing to the journal package of Akadémiai Kiadó: 100% |
| Subscription fee 2025 | Online subsscription: 880 EUR / 968 USD Print + online subscription: 1016 EUR / 1116 USD |
| Subscription Information | Online subscribers are entitled access to all back issues published by Akadémiai Kiadó for each title for the duration of the subscription, as well as Online First content for the subscribed content. |
| Purchase per Title | Individual articles are sold on the displayed price. |
| Acta Alimentaria | |
|---|---|
| Language | English |
| Size | B5 |
| Year of Foundation |
1972 |
| Volumes per Year |
1 |
| Issues per Year |
4 |
| Founder | Magyar Tudományos Akadémia  |
| Founder's Address |
H-1051 Budapest, Hungary, Széchenyi István tér 9. |
| Publisher | Akadémiai Kiadó |
| Publisher's Address |
H-1117 Budapest, Hungary 1516 Budapest, PO Box 245. |
| Responsible Publisher |
Chief Executive Officer, Akadémiai Kiadó |
| ISSN | 0139-3006 (Print) |
| ISSN | 1588-2535 (Online) |
Monthly Content Usage
| Abstract Views | Full Text Views | PDF Downloads | |
|---|---|---|---|
| Nov 2024 | 54 | 0 | 0 |
| Dec 2024 | 26 | 0 | 0 |
| Jan 2025 | 52 | 0 | 0 |
| Feb 2025 | 88 | 0 | 0 |
| Mar 2025 | 126 | 0 | 0 |
| Apr 2025 | 33 | 0 | 0 |
| May 2025 | 0 | 0 | 0 |
Author:
Authors:
, , , , , , , , , , , , and
Copyright Akadémiai Kiadó AKJournals is the trademark of Akadémiai Kiadó's journal publishing business branch.
Powered by PubFactory