Cargando…

Molecular Interactions between (−)-Epigallocatechin Gallate Analogs and Pancreatic Lipase

The molecular interactions between pancreatic lipase (PL) and four tea polyphenols (EGCG analogs), like (−)-epigallocatechin gallate (EGCG), (−)-gallocatechin gallate (GCG), (−)-epicatechin gallate (ECG), and (−)-epigallocatechin (EC), were studied from PL activity, conformation, kinetics and thermo...

Descripción completa

Detalles Bibliográficos
Autores principales: Wang, Shihui, Sun, Zeya, Dong, Shengzhao, Liu, Yang, Liu, Yun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4218840/
https://www.ncbi.nlm.nih.gov/pubmed/25365042
http://dx.doi.org/10.1371/journal.pone.0111143
_version_ 1782342485324857344
author Wang, Shihui
Sun, Zeya
Dong, Shengzhao
Liu, Yang
Liu, Yun
author_facet Wang, Shihui
Sun, Zeya
Dong, Shengzhao
Liu, Yang
Liu, Yun
author_sort Wang, Shihui
collection PubMed
description The molecular interactions between pancreatic lipase (PL) and four tea polyphenols (EGCG analogs), like (−)-epigallocatechin gallate (EGCG), (−)-gallocatechin gallate (GCG), (−)-epicatechin gallate (ECG), and (−)-epigallocatechin (EC), were studied from PL activity, conformation, kinetics and thermodynamics. It was observed that EGCG analogs inhibited PL activity, and their inhibitory rates decreased by the order of EGCG>GCG>ECG>EC. PL activity at first decreased rapidly and then slowly with the increase of EGCG analogs concentrations. α-Helix content of PL secondary structure decreased dependent on EGCG analogs concentration by the order of EGCG>GCG>ECG>EC. EGCG, ECG, and EC could quench PL fluorescence both dynamically and statically, while GCG only quenched statically. EGCG analogs would induce PL self-assembly into complexes and the hydrodynamic radii of the complexes possessed a close relationship with the inhibitory rates. Kinetics analysis showed that EGCG analogs non-competitively inhibited PL activity and did not bind to PL catalytic site. DSC measurement revealed that EGCG analogs decreased the transition midpoint temperature of PL enzyme, suggesting that these compounds reduced PL enzyme thermostability. In vitro renaturation through urea solution indicated that interactions between PL and EGCG analogs were weak and non-covalent.
format Online
Article
Text
id pubmed-4218840
institution National Center for Biotechnology Information
language English
publishDate 2014
publisher Public Library of Science
record_format MEDLINE/PubMed
spelling pubmed-42188402014-11-05 Molecular Interactions between (−)-Epigallocatechin Gallate Analogs and Pancreatic Lipase Wang, Shihui Sun, Zeya Dong, Shengzhao Liu, Yang Liu, Yun PLoS One Research Article The molecular interactions between pancreatic lipase (PL) and four tea polyphenols (EGCG analogs), like (−)-epigallocatechin gallate (EGCG), (−)-gallocatechin gallate (GCG), (−)-epicatechin gallate (ECG), and (−)-epigallocatechin (EC), were studied from PL activity, conformation, kinetics and thermodynamics. It was observed that EGCG analogs inhibited PL activity, and their inhibitory rates decreased by the order of EGCG>GCG>ECG>EC. PL activity at first decreased rapidly and then slowly with the increase of EGCG analogs concentrations. α-Helix content of PL secondary structure decreased dependent on EGCG analogs concentration by the order of EGCG>GCG>ECG>EC. EGCG, ECG, and EC could quench PL fluorescence both dynamically and statically, while GCG only quenched statically. EGCG analogs would induce PL self-assembly into complexes and the hydrodynamic radii of the complexes possessed a close relationship with the inhibitory rates. Kinetics analysis showed that EGCG analogs non-competitively inhibited PL activity and did not bind to PL catalytic site. DSC measurement revealed that EGCG analogs decreased the transition midpoint temperature of PL enzyme, suggesting that these compounds reduced PL enzyme thermostability. In vitro renaturation through urea solution indicated that interactions between PL and EGCG analogs were weak and non-covalent. Public Library of Science 2014-11-03 /pmc/articles/PMC4218840/ /pubmed/25365042 http://dx.doi.org/10.1371/journal.pone.0111143 Text en © 2014 Wang et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Wang, Shihui
Sun, Zeya
Dong, Shengzhao
Liu, Yang
Liu, Yun
Molecular Interactions between (−)-Epigallocatechin Gallate Analogs and Pancreatic Lipase
title Molecular Interactions between (−)-Epigallocatechin Gallate Analogs and Pancreatic Lipase
title_full Molecular Interactions between (−)-Epigallocatechin Gallate Analogs and Pancreatic Lipase
title_fullStr Molecular Interactions between (−)-Epigallocatechin Gallate Analogs and Pancreatic Lipase
title_full_unstemmed Molecular Interactions between (−)-Epigallocatechin Gallate Analogs and Pancreatic Lipase
title_short Molecular Interactions between (−)-Epigallocatechin Gallate Analogs and Pancreatic Lipase
title_sort molecular interactions between (−)-epigallocatechin gallate analogs and pancreatic lipase
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4218840/
https://www.ncbi.nlm.nih.gov/pubmed/25365042
http://dx.doi.org/10.1371/journal.pone.0111143
work_keys_str_mv AT wangshihui molecularinteractionsbetweenepigallocatechingallateanalogsandpancreaticlipase
AT sunzeya molecularinteractionsbetweenepigallocatechingallateanalogsandpancreaticlipase
AT dongshengzhao molecularinteractionsbetweenepigallocatechingallateanalogsandpancreaticlipase
AT liuyang molecularinteractionsbetweenepigallocatechingallateanalogsandpancreaticlipase
AT liuyun molecularinteractionsbetweenepigallocatechingallateanalogsandpancreaticlipase