Synthesis, Structure, Carbohydrate Enzyme Inhibition, Antioxidant Activity, In Silico Drug-Receptor Interactions and Drug-Like Profiling of the 5-Styryl-2-Aminochalcone Hybrids
The 2-amino-5-(3/4-fluorostyryl)acetophenones were prepared and reacted with benzaldehyde derivatives to afford the corresponding 5-styryl-2-aminochalcone hybrids. The <i>trans</i> geometry of the styryl and α,β-unsaturated carbonyl arms, and the presence of NH<sup>…</sup>O i...
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MDPI AG
2021-05-01
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| Online Access: | https://www.mdpi.com/1420-3049/26/9/2692 |
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| author | Malose J. Mphahlele Emmanuel Ndubuisi Agbo Yee Siew Choong |
| author_facet | Malose J. Mphahlele Emmanuel Ndubuisi Agbo Yee Siew Choong |
| author_sort | Malose J. Mphahlele |
| collection | DOAJ |
| description | The 2-amino-5-(3/4-fluorostyryl)acetophenones were prepared and reacted with benzaldehyde derivatives to afford the corresponding 5-styryl-2-aminochalcone hybrids. The <i>trans</i> geometry of the styryl and α,β-unsaturated carbonyl arms, and the presence of NH<sup>…</sup>O intramolecular hydrogen bond were validated using <sup>1</sup>H-NMR and X-ray data. The 2-amino-5-styrylacetophenones and their 5-styryl-2-aminochalcone derivatives were screened in vitro for their capability to inhibit α-glucosidase and/or α-amylase activities. Their antioxidant properties were evaluated in vitro through the 2,2-diphenyl-1-picrylhydrazyl (DPPH) and nitric oxide (NO) free radical scavenging assays. Kinetic studies of the most active derivatives from each series against α-glucosidase and/or α-amylase activities have been performed supported by molecular docking studies to determine plausible protein–ligand interactions on a molecular level. The key aspects of the pharmacokinetics of these compounds, i.e., absorption, distribution, metabolism, and excretion have also been simulated at theoretical level. The most active compounds from each series, namely, <b>2a</b> and <b>3e</b>, were evaluated for cytotoxicity against the normal monkey kidney cells (Vero cells) and the adenocarcinomic human epithelial (A549) cell line to establish their safety profile at least in vitro. |
| first_indexed | 2024-03-10T11:42:20Z |
| format | Article |
| id | doaj.art-6224b70469e54f938f2b5c07e6d63720 |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-10T11:42:20Z |
| publishDate | 2021-05-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-6224b70469e54f938f2b5c07e6d637202023-11-21T18:21:46ZengMDPI AGMolecules1420-30492021-05-01269269210.3390/molecules26092692Synthesis, Structure, Carbohydrate Enzyme Inhibition, Antioxidant Activity, In Silico Drug-Receptor Interactions and Drug-Like Profiling of the 5-Styryl-2-Aminochalcone HybridsMalose J. Mphahlele0Emmanuel Ndubuisi Agbo1Yee Siew Choong2Department of Chemistry, College of Science, Engineering and Technology, University of South Africa, Private Bag X06, Florida 1710, South AfricaDepartment of Chemistry, College of Science, Engineering and Technology, University of South Africa, Private Bag X06, Florida 1710, South AfricaInstitute for Research in Molecular Medicine (INFORMM), Universiti Sains Malaysia, Penang 11800, MalaysiaThe 2-amino-5-(3/4-fluorostyryl)acetophenones were prepared and reacted with benzaldehyde derivatives to afford the corresponding 5-styryl-2-aminochalcone hybrids. The <i>trans</i> geometry of the styryl and α,β-unsaturated carbonyl arms, and the presence of NH<sup>…</sup>O intramolecular hydrogen bond were validated using <sup>1</sup>H-NMR and X-ray data. The 2-amino-5-styrylacetophenones and their 5-styryl-2-aminochalcone derivatives were screened in vitro for their capability to inhibit α-glucosidase and/or α-amylase activities. Their antioxidant properties were evaluated in vitro through the 2,2-diphenyl-1-picrylhydrazyl (DPPH) and nitric oxide (NO) free radical scavenging assays. Kinetic studies of the most active derivatives from each series against α-glucosidase and/or α-amylase activities have been performed supported by molecular docking studies to determine plausible protein–ligand interactions on a molecular level. The key aspects of the pharmacokinetics of these compounds, i.e., absorption, distribution, metabolism, and excretion have also been simulated at theoretical level. The most active compounds from each series, namely, <b>2a</b> and <b>3e</b>, were evaluated for cytotoxicity against the normal monkey kidney cells (Vero cells) and the adenocarcinomic human epithelial (A549) cell line to establish their safety profile at least in vitro.https://www.mdpi.com/1420-3049/26/9/2692styryl-aminochalconesintramolecular hydrogen bondingα-glucosidaseα-amylaseantioxidantdrug-receptor interaction |
| spellingShingle | Malose J. Mphahlele Emmanuel Ndubuisi Agbo Yee Siew Choong Synthesis, Structure, Carbohydrate Enzyme Inhibition, Antioxidant Activity, In Silico Drug-Receptor Interactions and Drug-Like Profiling of the 5-Styryl-2-Aminochalcone Hybrids Molecules styryl-aminochalcones intramolecular hydrogen bonding α-glucosidase α-amylase antioxidant drug-receptor interaction |
| title | Synthesis, Structure, Carbohydrate Enzyme Inhibition, Antioxidant Activity, In Silico Drug-Receptor Interactions and Drug-Like Profiling of the 5-Styryl-2-Aminochalcone Hybrids |
| title_full | Synthesis, Structure, Carbohydrate Enzyme Inhibition, Antioxidant Activity, In Silico Drug-Receptor Interactions and Drug-Like Profiling of the 5-Styryl-2-Aminochalcone Hybrids |
| title_fullStr | Synthesis, Structure, Carbohydrate Enzyme Inhibition, Antioxidant Activity, In Silico Drug-Receptor Interactions and Drug-Like Profiling of the 5-Styryl-2-Aminochalcone Hybrids |
| title_full_unstemmed | Synthesis, Structure, Carbohydrate Enzyme Inhibition, Antioxidant Activity, In Silico Drug-Receptor Interactions and Drug-Like Profiling of the 5-Styryl-2-Aminochalcone Hybrids |
| title_short | Synthesis, Structure, Carbohydrate Enzyme Inhibition, Antioxidant Activity, In Silico Drug-Receptor Interactions and Drug-Like Profiling of the 5-Styryl-2-Aminochalcone Hybrids |
| title_sort | synthesis structure carbohydrate enzyme inhibition antioxidant activity in silico drug receptor interactions and drug like profiling of the 5 styryl 2 aminochalcone hybrids |
| topic | styryl-aminochalcones intramolecular hydrogen bonding α-glucosidase α-amylase antioxidant drug-receptor interaction |
| url | https://www.mdpi.com/1420-3049/26/9/2692 |
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