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Phenolic lipids affect the activity and conformation of acetylcholinesterase from Electrophorus electricus (Electric eel).

Stasiuk M, Janiszewska A, Kozubek A - Nutrients (2014)

Bottom Line: The observed effect distinctly depended on the chemical structure of the phenolic lipids that were available for interaction with the enzyme.All of the tested compounds reduced the activity of acetylcholinesterase.The degree of inhibition varied, showing a correlation with changes in the conformation of the enzyme tested by the intrinsic fluorescence of the Trp residues of the protein.

View Article: PubMed Central - PubMed

Affiliation: Department of Lipids and Liposomes, Faculty of Biotechnology, University of Wroclaw, Joliot-Curie 14a, Wroclaw 50-383, Poland. stasiuk@ibmb.uni.wroc.pl.

ABSTRACT
Phenolic lipids were isolated from rye grains, cashew nutshell liquid (CNSL) from Anacardium occidentale, and fruit bodies of Merrulius tremellosus, and their effects on the electric eel acetylcholinesterase activity and conformation were studied. The observed effect distinctly depended on the chemical structure of the phenolic lipids that were available for interaction with the enzyme. All of the tested compounds reduced the activity of acetylcholinesterase. The degree of inhibition varied, showing a correlation with changes in the conformation of the enzyme tested by the intrinsic fluorescence of the Trp residues of the protein.

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Inhibitory effect of phenolic lipids on acetylcholine (AChE) from E. electricus. (a) Phenolic resorcinolic and alkylphenolic lipids from A. occidentale. (b) Resorcinolic lipids from rye grain. (c) Merulinic acid from M. tremellosus. Data are given as means ± SD of three individual determinations, each performed in triplicate.
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nutrients-06-01823-f002: Inhibitory effect of phenolic lipids on acetylcholine (AChE) from E. electricus. (a) Phenolic resorcinolic and alkylphenolic lipids from A. occidentale. (b) Resorcinolic lipids from rye grain. (c) Merulinic acid from M. tremellosus. Data are given as means ± SD of three individual determinations, each performed in triplicate.

Mentions: Alkylphenolic (cardanol and anacardic acid) and resorcinolic lipids (cardol and methylcardol) from cashew nutshell liquid (CNSL) (Figure 1a), alkylresorcinols from rye grain (Figure 1b) and merulinic acid from Merulius tremellosus (Figure 1c) were tested for their in vitro inhibitory activity on AChE from Electrophorus electricus. The results are expressed as graphs (Figure 2a–c respectively). A decreased activity of AChE was observed in the presence of all of the tested phenolic lipids in the experimental media. The most effective decrease was observed after the addition of phenolic lipids from A. occidentale: anacardic acid, cardol and alkylphenol inhibited the enzyme activity almost completely. Resorcinolic lipids from rye bran demonstrated AChE activity inhibition that was related to the length of the alkyl chain present in the molecule. The increase in the number of carbon atoms in the chain caused a greater inhibition of the enzyme, but it never exceeded 70%. Merulinic acid caused AChE inhibition by max. 40%.


Phenolic lipids affect the activity and conformation of acetylcholinesterase from Electrophorus electricus (Electric eel).

Stasiuk M, Janiszewska A, Kozubek A - Nutrients (2014)

Inhibitory effect of phenolic lipids on acetylcholine (AChE) from E. electricus. (a) Phenolic resorcinolic and alkylphenolic lipids from A. occidentale. (b) Resorcinolic lipids from rye grain. (c) Merulinic acid from M. tremellosus. Data are given as means ± SD of three individual determinations, each performed in triplicate.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4042574&req=5

nutrients-06-01823-f002: Inhibitory effect of phenolic lipids on acetylcholine (AChE) from E. electricus. (a) Phenolic resorcinolic and alkylphenolic lipids from A. occidentale. (b) Resorcinolic lipids from rye grain. (c) Merulinic acid from M. tremellosus. Data are given as means ± SD of three individual determinations, each performed in triplicate.
Mentions: Alkylphenolic (cardanol and anacardic acid) and resorcinolic lipids (cardol and methylcardol) from cashew nutshell liquid (CNSL) (Figure 1a), alkylresorcinols from rye grain (Figure 1b) and merulinic acid from Merulius tremellosus (Figure 1c) were tested for their in vitro inhibitory activity on AChE from Electrophorus electricus. The results are expressed as graphs (Figure 2a–c respectively). A decreased activity of AChE was observed in the presence of all of the tested phenolic lipids in the experimental media. The most effective decrease was observed after the addition of phenolic lipids from A. occidentale: anacardic acid, cardol and alkylphenol inhibited the enzyme activity almost completely. Resorcinolic lipids from rye bran demonstrated AChE activity inhibition that was related to the length of the alkyl chain present in the molecule. The increase in the number of carbon atoms in the chain caused a greater inhibition of the enzyme, but it never exceeded 70%. Merulinic acid caused AChE inhibition by max. 40%.

Bottom Line: The observed effect distinctly depended on the chemical structure of the phenolic lipids that were available for interaction with the enzyme.All of the tested compounds reduced the activity of acetylcholinesterase.The degree of inhibition varied, showing a correlation with changes in the conformation of the enzyme tested by the intrinsic fluorescence of the Trp residues of the protein.

View Article: PubMed Central - PubMed

Affiliation: Department of Lipids and Liposomes, Faculty of Biotechnology, University of Wroclaw, Joliot-Curie 14a, Wroclaw 50-383, Poland. stasiuk@ibmb.uni.wroc.pl.

ABSTRACT
Phenolic lipids were isolated from rye grains, cashew nutshell liquid (CNSL) from Anacardium occidentale, and fruit bodies of Merrulius tremellosus, and their effects on the electric eel acetylcholinesterase activity and conformation were studied. The observed effect distinctly depended on the chemical structure of the phenolic lipids that were available for interaction with the enzyme. All of the tested compounds reduced the activity of acetylcholinesterase. The degree of inhibition varied, showing a correlation with changes in the conformation of the enzyme tested by the intrinsic fluorescence of the Trp residues of the protein.

Show MeSH
Related in: MedlinePlus