新規クマリン-トリアゾール-クマリン二量体のα-グルコシダーゼ活性

Ersin Şirin¹, Esra Sevimli¹, Gökçe Seyhan²

¹Department of Chemistry, Faculty of Engineering and Natural Sciences, Bursa Technical University, Bursa, Turkiye.

|January 9, 2026

Abstract:

Novel coumarin-triazole-coumarin dyads were synthesized and characterized, and their α-glycosidase inhibitory activities were evaluated spectrophotometrically. Compound 4e exhibited the most pronounced inhibitory effect, with an IC₅₀ value of 38.98 ± 0.77 μM. The IC₅₀ values for 4d and 4a were 93.55 ± 1.70 μM and 95.04 ± 3.55 μM, respectively. The Lineweaver-Burk plot showed that 4e inhibited α-glycosidase in a mixed type. In addition, the K _i value obtained from the Dixon plot was 19.95 ± 0.15 μM for α-glycosidase.

キーワード:

クマリン酵素阻害トリアゾール α-グルコシダーゼ

さらに関連する動画

09:10

Synthesis of Indoxyl-glycosides for Detection of Glycosidase Activities

Published on: May 27, 2015

7.1K

08:17

A High-Throughput Enzyme-Coupled Activity Assay to Probe Small Molecule Interaction with the dNTPase SAMHD1

Published on: April 16, 2021

2.8K

関連する概念動画

01:11

Aryldiazonium Salts to Azo Dyes: Diazo Coupling

3.6K

The reaction of weakly electrophilic aryldiazonium (also called arenediazonium) salts with highly activated aromatic compounds leads to the formation of products with an —N=N— link, called an azo linkage. This reaction, presented in Figure 1, is known as diazo coupling and occurs without the loss of the nitrogen atoms of the aryldiazonium salt. Highly activated aromatic compounds such as phenols or arylamines favor the diazo coupling reaction. The coupling generally occurs at the para...

3.6K

01:30

Enzyme Inhibition

91.5K

Inhibitors are molecules that reduce enzyme activity by binding to the enzyme. In a normally functioning cell, enzymes are regulated by a variety of inhibitors. Drugs and other toxins can also inhibit enzymes. Some inhibitors bind to the enzyme’s active site, while others inhibit enzymatic activity by binding to other sites on the protein structure.

91.5K