Preprint Article Version 1 Preserved in Portico This version is not peer-reviewed

Synthesis, Antioxidant, Anticholinesterase Activities and Molecular Docking Studies of coumaryl 1,3-selenazoles Derivatives

Version 1 : Received: 19 August 2020 / Approved: 20 August 2020 / Online: 20 August 2020 (07:26:34 CEST)

How to cite: Alias, N.Z.; Idris, M.H.M.; Somat, N.A.; Mahmud, N.; Hasan, S.; Wai, L.K.; Lazim, A.M.; Hassan, N.I. Synthesis, Antioxidant, Anticholinesterase Activities and Molecular Docking Studies of coumaryl 1,3-selenazoles Derivatives. Preprints 2020, 2020080438 (doi: 10.20944/preprints202008.0438.v1). Alias, N.Z.; Idris, M.H.M.; Somat, N.A.; Mahmud, N.; Hasan, S.; Wai, L.K.; Lazim, A.M.; Hassan, N.I. Synthesis, Antioxidant, Anticholinesterase Activities and Molecular Docking Studies of coumaryl 1,3-selenazoles Derivatives. Preprints 2020, 2020080438 (doi: 10.20944/preprints202008.0438.v1).

Abstract

Inhibition of acetylcholinesterase (AChE) enzyme is a known procedure to treat severe Alzheimer's disease through increasing the acetylcholine level in the brain and thus slowing down the progression of Alzheimer's symptoms. The approved medications are only considered as palliative and addressed some reported deficiencies. Therefore, the demand for safe and effective compounds is substantially increasing. A newly series of coumaryl 1,3-selenazoles derivatives was synthesized in four steps. Then, their antioxidant activities were evaluated using DPPH, ABTS cation radical scavenging assay and cupric reducing antioxidant capacities (CUPRAC). The anticholinesterase activities were evaluated using the Ellman method. Then, the docking studies were carried out to explain the possible correlation between in vitro anticholinesterase activity results and the ligand-receptor interactions. Ten new coumaryl 1,3-selenazoles (5a-5d series and 6a-6f series) derivatives were successfully synthesized. The DPPH radical scavenging assay showed that all tested compounds have IC50 value > 200 μM, for ABTS cation radical scavenging assay the IC50 value > 1000 μM and for CUPRAC assay the IC50 value > 200 μM. Compound 5c was found to be the most active compound against AChE and BChE in its series with IC50 value for AChE is 99.76 μM and IC50 for BChE is 140.28 μM while 6b exhibited the most potent inhibition in its series with IC50 value for AChE is 56.01 μM and IC50 for BChE is 121.34 μM. Besides, the docking studies showed that compound 5c and 6b formed π-π stacking interaction with aromatic residues at the active site of AChE and BChE, which is responsible for inhibiting the enzymes. This shows that the synthesized compounds contain skeletal structures that can interact and inhibit within the enzymes active site.

Subject Areas

acetylcholinesterase; antioxidant; Alzheimer; coumarin; selenazole

Comments (0)

We encourage comments and feedback from a broad range of readers. See criteria for comments and our diversity statement.

Leave a public comment
Send a private comment to the author(s)
Views 0
Downloads 0
Comments 0
Metrics 0


×
Alerts
Notify me about updates to this article or when a peer-reviewed version is published.
We use cookies on our website to ensure you get the best experience.
Read more about our cookies here.