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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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Interaction of E. electricus AChE with phenolic lipids. The graphs show the ratio of the fluorescence emission intensity at 310 nm of AChE versus lipid concentration. (a) Resorcinolic and alkylphenolic lipids from A. occidentale. (b) Resorcinolic lipids from rye grain. (c) Merulinic acid from M. tremellosus. F0 and F are the fluorescence intensity in the absence and in the presence of phenolic lipids, respectively. Data are given as means ± SD of three individual determinations, each performed in triplicate.
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nutrients-06-01823-f003: Interaction of E. electricus AChE with phenolic lipids. The graphs show the ratio of the fluorescence emission intensity at 310 nm of AChE versus lipid concentration. (a) Resorcinolic and alkylphenolic lipids from A. occidentale. (b) Resorcinolic lipids from rye grain. (c) Merulinic acid from M. tremellosus. F0 and F are the fluorescence intensity in the absence and in the presence of phenolic lipids, respectively. Data are given as means ± SD of three individual determinations, each performed in triplicate.

Mentions: Changes in the Trp emission of the investigated proteins in the presence of phenolic lipids depended on the chemical structures of compound applied. The more evident conformational modification was observed after treatment with alkylphenol (the value of F/F0 is three times greater, Figure 3a), AR 25:0 (the value of F/F0 is 2.5 times greater) and AR 19:0 (the value of F/F0 is 2 times higher, Figure 3b). The value of F/F0 decreases by about 80% after the addition of anacardic and merulinic acids (Figure 3a,c respectively). The change in fluorescence of Trp residues are smaller for the other lipids tested. No significant statistical differences were observed in fluorescence maxima position during our experiments.


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

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

Interaction of E. electricus AChE with phenolic lipids. The graphs show the ratio of the fluorescence emission intensity at 310 nm of AChE versus lipid concentration. (a) Resorcinolic and alkylphenolic lipids from A. occidentale. (b) Resorcinolic lipids from rye grain. (c) Merulinic acid from M. tremellosus. F0 and F are the fluorescence intensity in the absence and in the presence of phenolic lipids, respectively. 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-f003: Interaction of E. electricus AChE with phenolic lipids. The graphs show the ratio of the fluorescence emission intensity at 310 nm of AChE versus lipid concentration. (a) Resorcinolic and alkylphenolic lipids from A. occidentale. (b) Resorcinolic lipids from rye grain. (c) Merulinic acid from M. tremellosus. F0 and F are the fluorescence intensity in the absence and in the presence of phenolic lipids, respectively. Data are given as means ± SD of three individual determinations, each performed in triplicate.
Mentions: Changes in the Trp emission of the investigated proteins in the presence of phenolic lipids depended on the chemical structures of compound applied. The more evident conformational modification was observed after treatment with alkylphenol (the value of F/F0 is three times greater, Figure 3a), AR 25:0 (the value of F/F0 is 2.5 times greater) and AR 19:0 (the value of F/F0 is 2 times higher, Figure 3b). The value of F/F0 decreases by about 80% after the addition of anacardic and merulinic acids (Figure 3a,c respectively). The change in fluorescence of Trp residues are smaller for the other lipids tested. No significant statistical differences were observed in fluorescence maxima position during our experiments.

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