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Evaluation of a flavonoids library for inhibition of pancreatic α-amylase towards a structure-activity relationship.
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- Additional Information
- Source:
Publisher: Taylor & Francis Country of Publication: England NLM ID: 101150203 Publication Model: Print Cited Medium: Internet ISSN: 1475-6374 (Electronic) Linking ISSN: 14756366 NLM ISO Abbreviation: J Enzyme Inhib Med Chem Subsets: MEDLINE
- Publication Information:
Original Publication: Basingstoke, UK : Taylor & Francis, c2002-
- Subject Terms:
- Abstract:
α-Amylase has been considered an important therapeutic target for the management of type 2 diabetes mellitus (T2DM), decreasing postprandial hyperglycaemia (PPHG). In the present work, a panel of 40 structurally related flavonoids was tested, concerning their ability to inhibit α-amylase activity, using a microanalysis screening system, an inhibitory kinetic analysis and molecular docking calculations. From the obtained results, it was possible to observe that the flavone with a -Cl ion at 3-position of C-ring, an -OH group at 3'- and 4'- positions of B-ring and at 5- and 7- positions of A-ring and the C2 = C3 double bond, was the most active tested flavonoid, through competitive inhibition. In conclusion, some of the tested flavonoids have shown promising inhibition of α-amylase and may be considered as possible alternatives to the modulation of T2DM.
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- Contributed Indexing:
Keywords: ; diabetes; docking; flavonoids; α-Amylase inhibition
- Accession Number:
0 (Flavonoids)
0 (Glycoside Hydrolase Inhibitors)
0 (Small Molecule Libraries)
EC 3.2.1.1 (Pancreatic alpha-Amylases)
- Publication Date:
Date Created: 20190207 Date Completed: 20190222 Latest Revision: 20200225
- Publication Date:
20221213
- Accession Number:
PMC6366418
- Accession Number:
10.1080/14756366.2018.1558221
- Accession Number:
30724629
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