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Paper ID:IJSREM66715

PHYTOCHEMICAL CHARACTERIZATION AND IN VITRO EVALUATION OF α-AMYLASE AND α-GLUCOSIDE INHIBITRY POTENTIAL OF BERGERA KOENIGII LEAF EXTRACT FOR THE MANAGEMENT OF TYPE 2 DIABETES MELLITUS

Stream/Area:

-

Subject:

-

Paper ID:

IJSREM66715

Volume:

10 |

8 |

Aug 2026

Pages:

1-4

Publication Frequency:

Monthly (12 issues per year)

DOI
Digital Object Identifier
10.55041/IJSREM66715

License:International Journal of Scientific Research in Engineering and Management follows the Creative Commons Attribution 4.0 (CC BY 4.0) License, allowing free use and distribution with proper attribution.

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Authors

NS

N. Sundharraj

pharmacology

Sri Vijay Vidyalaya College of Pharmacy, Dharmapuri, Tamil Nadu, India

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RS

R. Suganya

pharmacology

Sri Vijay Vidyalaya College of Pharmacy, Dharmapuri, Tamil Nadu, India

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PS

P. Subhashini

pharmacology

Sri Vijay Vidyalaya College of Pharmacy, Dharmapuri, Tamil Nadu, India

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Mentors

SA

S. Ananthi

pharmacology

Sri Vijay Vidyalaya College of Pharmacy, Dharmapuri, Tamil Nadu, India

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Abstract

Type 2 diabetes mellitus (T2DM) is a chronic metabolic disorder driven by insulin resistance and progressive pancreatic β-cell dysfunction, and accounts for 90-95% of all diabetes cases worldwide. Inhibition of carbohydrate-digesting enzymes (α-amylase and α-glucosidase) and of dipeptidyl peptidase-4 (DPP-4), which degrades the incretin hormones GLP-1 and GIP, are established therapeutic strategies for improving postprandial glycaemic control. This study evaluated the in vitro antidiabetic potential of an ethanolic extract of Bergera koenigii (curry leaf) leaves against these three enzyme targets. Leaves were authenticated, shade-dried, powdered and extracted by Soxhlet extraction with ethanol; preliminary GC-MS screening and phytochemical analysis were performed. α-Amylase and α-glucosidase inhibitory activities were assessed spectrophotometrically over 200-1000 μg/mL against acarbose, and DPP-4 inhibitory activity was assessed over 25-400 μg/mL against sitagliptin. The extract showed concentration-dependent inhibition in all three assays, reaching 80.89% α-amylase inhibition (IC₅₀ 638 μg/mL, versus acarbose 90.25%, IC₅₀ 518 μg/mL), 80.89% α-glucosidase inhibition (IC₅₀ 633 μg/mL, versus acarbose 90.25%, IC₅₀ 518 μg/mL), and 78% DPP-4 inhibition at 400 μg/mL (versus 85% for sitagliptin). While less potent than the reference standards, the extract demonstrated substantial, concentration-dependent activity across all three mechanistically relevant targets, supporting its potential as a natural multi-target antidiabetic agent warranting further investigation.

KEYWORDS

Bergera koenigii; curry leaf; Type 2 diabetes mellitus; α-amylase inhibition; α-glucosidase inhibition; DPP-4 inhibition; IC50.

Cite This Article

N. Sundharraj, R. Suganya, P. Subhashini, S. Ananthi, "PHYTOCHEMICAL CHARACTERIZATION AND IN VITRO EVALUATION OF α-AMYLASE AND α-GLUCOSIDE INHIBITRY POTENTIAL OF BERGERA KOENIGII LEAF EXTRACT FOR THE MANAGEMENT OF TYPE 2 DIABETES MELLITUS," International Journal of Scientific Research in Engineering and Management, vol. 10, no. 8, pp. 1-4, Aug 2026. https://doi.org/10.55041/IJSREM66715

Full Article/Conclusion

The ethanolic extract of Bergera koenigii leaves demonstrated concentration-dependent in vitro inhibitory activity against three mechanistically distinct, clinically relevant antidiabetic targets: α-amylase (80.89% inhibition, IC₅₀ 638 μg/mL), α-glucosidase (80.89% inhibition, IC₅₀ 633 μg/mL), and DPP-4 (78% inhibition at 400 μg/mL). Although less potent than the reference standards acarbose and sitagliptin, this multi-target enzyme-inhibitory profile supports the traditional use of curry leaf in diabetes management and its potential as a source of natural antidiabetic constituents. The findings represent preliminary in vitro evidence rather than proof of clinical efficacy. Future work should include triplicate DPP-4 measurements with reported SD, nonlinear regression to establish a DPP-4 IC₅₀, expanded concentration ranges bracketing the IC₅₀ values, appropriate statistical significance testing, and bioassay-guided fractionation to identify the specific phytoconstituents responsible for the observed activity.

References

[1]  International Diabetes Federation. IDF Diabetes Atlas. 10th ed. Brussels: International Diabetes Federation; 2021. [2]  American Diabetes Association Professional Practice Committee. Classification and diagnosis of diabetes: Standards of Care in Diabetes-2024. Diabetes Care. 2024;47(Suppl 1):S20-S42. [3]  DeFronzo RA. From the triumvirate to the ominous octet: a new paradigm for the treatment of type 2 diabetes mellitus. Diabetes. 2009;58(4):773-795. [4]  Drucker DJ. The biology of incretin hormones. Cell Metab. 2006;3(3):153-165. [5]  Drucker DJ, Nauck MA. The incretin system: GLP-1 receptor agonists and DPP-4 inhibitors in type 2 diabetes. Lancet. 2006;368(9548):1696-1705. [6]  Mulvihill EE, Drucker DJ. Pharmacology, physiology, and mechanisms of action of dipeptidyl peptidase-4 inhibitors. Endocr Rev. 2014;35(6):992-1019. [7]  Deacon CF. Dipeptidyl peptidase-4 inhibition with sitagliptin: a new therapy for type 2 diabetes. Expert Opin Pharmacother. 2007;8(13):2059-2071. [8]  Holst JJ, Deacon CF. Inhibition of the activity of dipeptidyl-peptidase IV as a treatment for type 2 diabetes. Diabetes. 1998;47(11):1663-1670. [9]  Mentlein R. Dipeptidyl-peptidase IV (CD26)-role in inactivation of regulatory peptides. Regul Pept. 1999;85(1):9-24. [10]    Tundis R, Loizzo MR, Menichini F. Natural products as α-amylase and α-glucosidase inhibitors and their hypoglycaemic potential in the treatment of diabetes: an update. Mini Rev Med Chem. 2010;10(4):315-331.

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Publication Date

8/12/2026

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