Experimental and bioinformatic investigation of the anticholinesterase effect of honey bee venom

Aslani , Mohammad Kazem; Lotfi , Safa; Rezvannejad, Elham; Zare Mirakabadi , Abbas; Torkzadeh Mahani , Masoud

doi:10.22034/aer.2.4.57

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Experimental and bioinformatic investigation of the anticholinesterase effect of honey bee venom

Mohammad Kazem Aslani

, Safa Lotfi Dr. ^*

, Elham Rezvannejad Dr.

, Abbas Zare Mirakabadi Dr.

, Masoud Torkzadeh Mahani Dr.

Abstract: (417 Views)

Introduction: Alzheimer’s disease (AD) is the most common form of dementia in the elderly, characterized as a progressive neurodegenerative disorder. One of the primary strategies employed to achieve a relative improvement in AD symptoms is the administration of cholinesterase inhibitors (acetylcholinesterase and butyrylcholinesterase). Natural compounds, such as extracts from plants, fungi, algae, and animal venoms, contain various bioactive compounds that are of significant importance for drug discovery in many diseases, including AD, due to their low side effects and appropriate efficacy. Honey bee venom is a natural substance with diverse active compounds exhibiting a wide range of biological properties, and it has demonstrated therapeutic effects against various diseases, including Alzheimer’s.
Materials & Methods: In this study, the cholinesterase inhibitory potential of honey bee venom was investigated using the Elman assay. Subsequently, the binding sites of the most important peptidic and protein components of honey bee venom (melittin, apamin, mast cell degranulating peptide (MCD), phospholipase A2, hyaluronidase) on acetylcholinesterase were predicted using the HADDOCK protein-protein docking simulation server. The LigPlot software was utilized for analyzing the obtained results.
Results: The results indicated that honey bee venom exhibited a significantly better inhibitory effect on acetylcholinesterase, the primary cholinesterase, compared to butyrylcholinesterase. The simulation results revealed that melittin, MCD, and hyaluronidase could form hydrogen bonds with certain amino acid residues within the peripheral anionic site (PAS) of the enzyme. This interaction not only inhibits enzyme activity but also prevents the formation and aggregation of amyloid-beta.
Conclusion: Among the studied compounds, melittin, the main and most abundant component of honey bee venom, showed the best binding energy. Collectively, the findings of this study suggest that honey bee venom is a suitable candidate for the identification, design, and introduction of novel anticholinesterase drugs for the treatment of Alzheimer’s disease.

Keywords: Alzheimer’s disease, Anticholinesterase activity, Honey bee venom, Protein-protein docking, HADDOCK server

Full-Text [PDF 1232 kb] (111 Downloads)

Type of Study: Research | Subject: Special

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