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Differential inhibition of human erythrocyte acetylcholinesterase by polyphenols epigallocatechin‐3‐gallate and resveratrol. Relevance of the membrane‐bound form
Author(s) -
Salazar Paula B.,
de Athayde Moncorvo Collado Alejandro,
CanalMartínez Verónica,
Minahk Carlos J.
Publication year - 2016
Publication title -
biofactors
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.204
H-Index - 94
eISSN - 1872-8081
pISSN - 0951-6433
DOI - 10.1002/biof.1322
Subject(s) - acetylcholinesterase , resveratrol , epigallocatechin gallate , chemistry , aché , gallate , enzyme , biochemistry , polyphenol , flavonoid , red blood cell , membrane , antioxidant , nuclear chemistry
The activity of acetylcholinesterase (AChE) from human erythrocytes was tested in the presence of the phenolic compounds resveratrol and epigallocatechin‐3‐gallate (EGCG). Even though the stilbene barely changed this enzymatic activity, EGCG did inhibit AChE. Importantly, it preferentially acted on the membrane‐bound enzyme rather than on its soluble form. Actually, it was shown that this flavonoid may bind to the red blood cell membrane surface, which may improve the interaction between EGCG and AChE. Therefore, caution should be taken when screening AChE inhibitors. In fact, testing compounds with the soluble form of the enzyme may underestimate the activity of some of these potential inhibitors, hence it would be advisable not to use them as a sole model system for screening. Moreover, erythrocyte AChE is proposed as a good model for these enzymatic assays. © 2016 BioFactors, 43(1):73–81, 2017