SCREENING OF METHANOL EXTRACT OF PICRALIMA NITIDA SEEDS FOR Α-AMYLASE AND Α-GLUCOSIDASE INHIBITORS THROUGH IN-VITRO AND MOLECULAR DOCKING ANALYSES


Lawal J Biomed & App Sci FUD (2024) 3:2

Keywords: Picralima nitida; alpha amylase; alpha glucosidase; molecular docking; diabetes mellitus

2025-05-16 DOI: JOBASFUD_2024_3_2_023

Abstract


Background: The activities of α-amylase and α-glucosidase have been linked to postprandial hyperglycaemia, which, if not properly controlled, can lead to diabetes mellitus. Diabetes mellitus is a metabolic disorder characterised by persistent high blood sugar levels due to the body's inability to produce or effectively use insulin. If this condition is not properly managed, it can lead to various complications such as cardiovascular disease, nephropathy, neuropathy, retinopathy, and an increased risk of infections. Synthetic drugs used to treat this condition have been found to have harmful effects on the kidneys, heart, and liver functions in some patients. Consequently, there is a need to find natural products with minimal side effects to manage this disorder. This study examined various fractions of methanol extract from Picralima nitida seeds for their ability to inhibit α-amylase and α-glucosidase. Results: The most potent fraction was identified as PF6 from column chromatography, with the least IC50 of 48.17±1.61 and 25.32±1.81 μg/mL against α-amylase and α-glucosidase, respectively. Sub-fraction 4 (SF4) obtained from PF6 showed the highest potency with an IC50 of 52.48±6.54 and 30.20±2.02 against α-amylase and α-glucosidase, respectively. The standard drug acarbose exhibited IC50 values of 25.34±1.22 and 22.28±2.03, making it more potent than the fractions and Sub-fractions against the two enzymes. FTIR analysis revealed the presence of C=O, O-H, C-O, C=C, C-N, Ar-CH, C=S, Ar-O-C, CH2, and CH3 functional groups. LCMS analysis tentatively identified genipin, genistein, cirantin, bezafibrate, and usnic acid in SF4. Molecular docking analysis revealed that cirantin and genistein are potent inhibitors for α-amylase and α-glucosidase, with docking scores of -7.9928 and -8.8359 kcal/mol, respectively. At the same time, acarbose exhibited scores of -9.0021 and -8.3366 kcal/mol against the two enzymes. The identified compounds have exhibited strong molecular docking interactions with α-amylase and α-glucosidase, indicating their potential to inhibit these two enzymes effectively. Conclusion, further research should be conducted on these compounds, particularly cirantin and genistein, as they are potentially used as antidiabetic agents due to their inhibitory effects on carbohydrate digestive enzymes.

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