AI Article Synopsis
- The study focused on α-Glucosidase, an enzyme that affects blood sugar levels after meals, and analyzed compounds from a certain source along with their isoxazoline derivatives for their inhibitory effects.
- Among the thirteen compounds tested, compounds 1, 3a, and 3j showed significant inhibition of α-glucosidase with lower IC values than the commonly used drug, acarbose.
- The research included kinetic studies revealing different binding mechanisms for each compound, showing strong interactions and favorable binding affinities, highlighting their potential as effective inhibitors against α-glucosidase.
Article Abstract
α-Glucosidase, an enzyme involved in post-prandial hyperglycaemia, was used as a target to study the effect of compound(s) isolated from and its isoxazoline derivatives. Among thirteen compounds screened, compounds 1, 3a and 3j exhibited significant inhibition with IC values of 63.42, 61.36 and 58.89 µg/mL, respectively, outperforming acarbose (71.72 µg/mL). Kinetic studies revealed competitive binding for compound 1 and uncompetitive/non-competitive binding for 3a and 3j. Fluorescence quenching showed a linear relationship between / at different inhibitor concentrations. The binding sites in α-glucosidase were ≤ 1. The binding constants 3a (0.7307) > 3j (0.6563) > 1 (0.5415) displayed strong interactions. Docking study revealed binding affinities; 3j (-8.9) > 3a (-7.7) > 1 (-7), and acarbose, 1, 3a and 3j had ARG-312, PHE-157 interactions in common to α-glucosidase. The toxicity profile showed compounds fell in classes IV and V. Overall, the results indicate that compounds 1, 3a and 3j are effective against α-glucosidase.
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| http://dx.doi.org/10.1080/14786419.2024.2352140 | DOI Listing |
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