Inhibition of catalase by tea catechins in free and cellular state: a biophysical approach.

Tea flavonoids bind to variety of enzymes and inhibit their activities. In the present study, binding and inhibition of catalase activity by catechins with respect to their structure-affinity relationship has been elucidated. Fluorimetrically determined binding constants for (-)-epigallocatechin gal...

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Autores principales:	Sandip Pal, Subrata Kumar Dey, Chabita Saha
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/309a9872cbcd407780d4b554a1c7cdec
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spelling	oai:doaj.org-article:309a9872cbcd407780d4b554a1c7cdec2021-11-25T06:08:23ZInhibition of catalase by tea catechins in free and cellular state: a biophysical approach.1932-620310.1371/journal.pone.0102460https://doaj.org/article/309a9872cbcd407780d4b554a1c7cdec2014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/25025898/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Tea flavonoids bind to variety of enzymes and inhibit their activities. In the present study, binding and inhibition of catalase activity by catechins with respect to their structure-affinity relationship has been elucidated. Fluorimetrically determined binding constants for (-)-epigallocatechin gallate (EGCG) and (-)-epicatechin gallate (ECG) with catalase were observed to be 2.27×106 M(-1) and 1.66×106 M(-1), respectively. Thermodynamic parameters evidence exothermic and spontaneous interaction between catechins and catalase. Major forces of interaction are suggested to be through hydrogen bonding along with electrostatic contributions and conformational changes. Distinct loss of α-helical structure of catalase by interaction with EGCG was captured in circular dichroism (CD) spectra. Gallated catechins demonstrated higher binding constants and inhibition efficacy than non-gallated catechins. EGCG exhibited maximum inhibition of pure catalase. It also inhibited cellular catalase in K562 cancer cells with significant increase in cellular ROS and suppression of cell viability (IC50 54.5 µM). These results decipher the molecular mechanism by which tea catechins interact with catalase and highlight the potential of gallated catechin like EGCG as an anticancer drug. EGCG may have other non-specific targets in the cell, but its anticancer property is mainly defined by ROS accumulation due to catalase inhibition.Sandip PalSubrata Kumar DeyChabita SahaPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 7, p e102460 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Sandip Pal Subrata Kumar Dey Chabita Saha Inhibition of catalase by tea catechins in free and cellular state: a biophysical approach.
description	Tea flavonoids bind to variety of enzymes and inhibit their activities. In the present study, binding and inhibition of catalase activity by catechins with respect to their structure-affinity relationship has been elucidated. Fluorimetrically determined binding constants for (-)-epigallocatechin gallate (EGCG) and (-)-epicatechin gallate (ECG) with catalase were observed to be 2.27×106 M(-1) and 1.66×106 M(-1), respectively. Thermodynamic parameters evidence exothermic and spontaneous interaction between catechins and catalase. Major forces of interaction are suggested to be through hydrogen bonding along with electrostatic contributions and conformational changes. Distinct loss of α-helical structure of catalase by interaction with EGCG was captured in circular dichroism (CD) spectra. Gallated catechins demonstrated higher binding constants and inhibition efficacy than non-gallated catechins. EGCG exhibited maximum inhibition of pure catalase. It also inhibited cellular catalase in K562 cancer cells with significant increase in cellular ROS and suppression of cell viability (IC50 54.5 µM). These results decipher the molecular mechanism by which tea catechins interact with catalase and highlight the potential of gallated catechin like EGCG as an anticancer drug. EGCG may have other non-specific targets in the cell, but its anticancer property is mainly defined by ROS accumulation due to catalase inhibition.
format	article
author	Sandip Pal Subrata Kumar Dey Chabita Saha
author_facet	Sandip Pal Subrata Kumar Dey Chabita Saha
author_sort	Sandip Pal
title	Inhibition of catalase by tea catechins in free and cellular state: a biophysical approach.
title_short	Inhibition of catalase by tea catechins in free and cellular state: a biophysical approach.
title_full	Inhibition of catalase by tea catechins in free and cellular state: a biophysical approach.
title_fullStr	Inhibition of catalase by tea catechins in free and cellular state: a biophysical approach.
title_full_unstemmed	Inhibition of catalase by tea catechins in free and cellular state: a biophysical approach.
title_sort	inhibition of catalase by tea catechins in free and cellular state: a biophysical approach.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/309a9872cbcd407780d4b554a1c7cdec
work_keys_str_mv	AT sandippal inhibitionofcatalasebyteacatechinsinfreeandcellularstateabiophysicalapproach AT subratakumardey inhibitionofcatalasebyteacatechinsinfreeandcellularstateabiophysicalapproach AT chabitasaha inhibitionofcatalasebyteacatechinsinfreeandcellularstateabiophysicalapproach
_version_	1718414093558218752

Inhibition of catalase by tea catechins in free and cellular state: a biophysical approach.

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