α-glucosidase and glycation inhibitory effects of costus speciosus leaves
Handunge Kumudu Irani Perera1, Walgama Kankanamlage Vindhya Kalpani Premadasa2,3, Jeyakumaran Poongunran4,5
1Department of Biochemistry, Faculty of Medicine, University of Peradeniya, Peradeniya, Sri Lanka. kumudup@pdn.ac.lk.
Background:
Hyperglycaemia is a salient feature of poorly controlled diabetes mellitus. Rate of protein glycation is increased with hyperglycaemia leading to long term complications of diabetes. One approach of controlling blood glucose in diabetes targets at reducing the postprandial spikes of blood glucose. The objectives of this study were to assess the in vitro inhibitory effects of Costus speciosus (COS) leaves on α-amylase and α-glucosidase activities, fructosamine formation, protein glycation and glycation-induced protein cross-linking.
Methods:
Methanol extracts of COS leaves were used. Inhibitory effects on enzyme activities were measured using porcine pancreatic α-amylase and α-glucosidase from Saccharomyces cerevisiae in the presence of COS extract. Percentage inhibition of the enzymes and the IC50 values were determined. In vitro protein glycation inhibitory effect of COS leaves on early and late glycation products were measured using bovine serum albumin or chicken egg lysozyme with fructose. Nitroblue tetrazolium was used to assess the relative concentration of fructosamine and polyacrylamide gel electrophoresis was used to assess the degree of glycation and protein cross-linking in the reaction mixtures.
Results:
α-Glucosidase inhibitory activity was detected in COS leaves with a IC50 of 67.5 μg/ml which was significantly lower than the IC50 value of Acarbose (p < 0.01). Amylase inhibitory effects occurred at a comparatively higher concentration of extract with a IC50 of 5.88 mg/ml which was significantly higher than the IC50 value of Acarbose (p < 0.01). COS (250 μg/ml) demonstrated inhibitory effects on fructosamine formation and glycation induced protein cross-linking which were in par with 1 mg/ml aminoguanidine were detected.
Conclusion:
Methanol extracts of COS leaves demonstrated in vitro inhibitory activities on α-glucosidase, fructosamine formation, glycation and glycation induced protein cross-linking. These findings provide scientific evidence to support the use of COS leaves for hypoglycemic effects with an added advantage in slowing down protein glycation.
Insights
Costus speciosus (COS) leaves show significant potential in managing hyperglycemia by inhibiting alpha-glucosidase and reducing protein glycation. These findings support its use for hypoglycemic effects and preventing diabetes complications.
Area of Science:
- Biochemistry
- Pharmacology
- Phytomedicine
Background:
- Hyperglycemia in diabetes elevates protein glycation, leading to long-term complications.
- Controlling postprandial blood glucose spikes is a key strategy in diabetes management.
- Costus speciosus (COS) is explored for its potential hypoglycemic and anti-glycation properties.
Purpose of the Study:
- To evaluate the in vitro inhibitory effects of COS leaves on key enzymes involved in glucose metabolism.
- To assess the impact of COS on protein glycation and related processes.
- To provide scientific evidence for the traditional use of COS in managing diabetes.
Main Methods:
- Methanol extracts of COS leaves were used to test inhibitory effects on porcine pancreatic alpha-amylase and Saccharomyces cerevisiae alpha-glucosidase.
- In vitro assays measured inhibition of fructosamine formation and glycation-induced protein cross-linking using bovine serum albumin and chicken egg lysozyme.
- Nitroblue tetrazolium and polyacrylamide gel electrophoresis were employed to quantify glycation markers.
Main Results:
- COS leaves exhibited significant alpha-glucosidase inhibitory activity (IC50 = 67.5 μg/ml), outperforming Acarbose.
- Alpha-amylase inhibition by COS was less potent (IC50 = 5.88 mg/ml) compared to Acarbose.
- COS demonstrated notable inhibition of fructosamine formation and protein cross-linking, comparable to aminoguanidine.
Conclusions:
- Methanol extracts of COS leaves possess significant in vitro inhibitory activity against alpha-glucosidase.
- COS effectively reduces fructosamine formation and inhibits glycation-induced protein cross-linking.
- These results support the hypoglycemic potential of COS leaves and their role in mitigating diabetes-related protein damage.
More Related Videos
13:35Structural Biology and Analytical Chemistry Approaches for Characterizing C-Glycoside Metabolic Enzymes in Human Gut Microbiota
Published on: May 23, 2025
10:26Author Spotlight: Integrating Biochemical Functions of β-Glucanases and Peroxidase Enzymes in Wheat-RWA Interaction
Published on: July 26, 2024
Related Concept Videos
01:19Oral Hypoglycemic Agents: α-Glucosidase Inhibitors
Acarbose and miglitol are...
01:23Dipeptidyl Peptidase 4 Inhibitors
01:06Oral Hypoglycemic Agents: Glinides