Benzo[a]pyrene and Benzo[a]pyrene-7,8-dihydrodiol-9,10-epoxide induced locomotor and reproductive senescence and altered biochemical parameters of oxidative damage in Canton-S Drosophila melanogaster

Johnson, Titilayo Omolara; Abolaji, Amos O.; Omale, Simeon; Longdet, Ishaya Yohanna; Kutshik, Richard Joseph; Oyetayo, Bolaji O.; Adegboyega, Abayomi Emmanuel; Sagay, Atiene S.

doi:10.1016/j.toxrep.2021.03.001

Cited by 14 publications

(23 citation statements)

References 43 publications

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“…Acetylcholinesterase (AChE) is an enzyme that terminates synaptic transmission at cholinergic synapses through its swift hydrolysis of acetylcholine, a neurotransmitter, and it has been an effective target for a wide array of chemical agents including the anti-Alzheimer drugs and insecticides [ 1 , 3 ]. Insecticide development is a very important aspect of the global fight against epidemics and pandemics.…”

Section: Discussionmentioning

confidence: 99%

“…Percentage negative geotaxis is a measure of the locomotor performance of flies based on the number of flies that climbed beyond a defined distance within a specific time or the amount of time it takes to climb a specified height [ 1 ]. Reduction in negative geotaxis which is usually accompanied by a decreased AChE activity is regarded as an indicator of the neurotoxicity of chemicals [ 12 ].…”

Section: Discussionmentioning

confidence: 99%

“…A negative Geotaxis assay was performed as previously described by Johnson et al [ 1 ]. The flies were treated with the extract as described above for 45 min after which they were transferred into empty treatment vials.…”

Section: Methodsmentioning

confidence: 99%

“…Acetylcholinesterase is a cholinergic enzyme that catalyses the breakdown of acetylcholine to acetic acid and choline, thereby terminating nerve transmission at the synapses [ 1 ]. Acetylcholine is the major neurotransmitter found in the central nervous system (CNS) of both vertebrates and invertebrates alongside other transmitters, and the regulation of its activity by AChE-catalysed hydrolysis is essential for the normal functioning and/or survival of these animals.…”

Section: Introductionmentioning

confidence: 99%

“…Due to its involvement in the termination of impulse transmission in insects [ 2 ], AChE has functioned as the target of many insecticides including organophosphates and carbamates [ 3 ]. Inhibition of AChE by these insecticides causes the accumulation of acetylcholine in the synapses, making acetylcholine receptors to be permanently open and resulting in some toxicological outcomes [ 1 , 4 ].…”

Section: Introductionmentioning

confidence: 99%

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Biochemical evaluation and molecular docking assessment of Cymbopogon citratus as a natural source of acetylcholine esterase (AChE)- targeting insecticides

Johnson¹,

Ojo²,

Ikiriko³

et al. 2021

Biochemistry and Biophysics Reports

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Acetylcholinesterase (AChE) has been an effective target for insecticide development which is a very important aspect of the global fight against insect-borne diseases. The drastic reduction in the sensitivity of insects to AChE-targeting insecticides like organophosphates and carbamates have increased the need for insecticides of natural origin. In this study, we used Drosophila melanogaster as a model to investigate the insecticidal and AChE inhibitory potentials of Cymbopogon citratus and its bioactive compounds. Flies were exposed to 100 and 200 mg/mL C . citratus leaf extract for a 3-h survival assay followed by 45 min exposure for negative geotaxis and biochemical assays. Molecular docking analysis of 45 bioactive compounds of the plant was conducted against Drosophila melanogaster AChE (DmAChE). Exposure to C. citratus significantly reduced the survival rate of flies throughout the exposure period and this was accompanied by a significant decrease in percentage negative geotaxis, AChE activity, catalase activity, total thiol level and a significant increase in glutathione-S-transferase (GST) activity. The bioactive compounds of C. citratus showed varying levels of binding affinities for the enzyme. (+)-Cymbodiacetal scored highest (−9.407 kcal/mol) followed by proximadiol (−8.253 kcal/mol), geranylacetone (−8.177 kcal/mol), and rutin (−8.148 kcal/mol). The four compounds occupied the same binding pocket and interacted with important active site amino acid residues as the co-crystallized ligand (1qon). These compounds could be responsible for the insecticidal and AChE inhibitory potentials of C. citratus and they could be further explored in the development of AChE-targeting insecticides.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%