Glycation and oxidative stress are the major contributing factors responsible for diabetes and its secondary complications. Aminoguanidine, a hydrazine derivative, is the only approved drug that reduces glycation with its known side effects. As a result, research into medicinal plants with antioxidant and antiglycation properties is beneficial in treating diabetes and its consequences. This investigation aimed to examine the efficacy of the aqueous extract of seeds against the D-ribose-induced glycation system. The suppression of α-amylase and α-glucosidase enzymes were used to assess the antidiabetic capacity. UV-Visible, fluorescence, and FTIR spectroscopy were used to characterize the seed extract and its efficacy in preventing glycation. The inhibition of albumin glycation, fluorescent advanced glycation end products (AGEs) formation, thiol oxidation, and amyloid formation were used to evaluate the extracts' antiglycation activity. In addition, the extent of glycoxidative DNA damage was analyzed using agarose gel electrophoresis. The IC for the extract in the α-amylase and α-glucosidase enzyme inhibition assays were approximately 1.39 ± 0.016 and 1.01 ± 0.022 mg/mL, respectively. Throughout the investigation, it was found that the aqueous extract of seeds (NSAE) inhibited the level of ketoamine, exerted a considerable drop in fluorescence intensity, and reduced carbonyl production and thiol modification when added to the D-ribose-induced glycation system. In addition, a reduction in the BSA-cross amyloid formation was seen in the Congo red, thioflavin T assay, and electrophoretic techniques. NSAE also exhibited a strong capability for DNA damage protection. It can be concluded that could be used as a natural antidiabetic, antiglycation treatment and a cost-effective and environmentally friendly source of powerful bioactive chemicals.
Download full-text PDF |
Source |
---|---|
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9788360 | PMC |
http://dx.doi.org/10.3390/medicina58121816 | DOI Listing |
Int J Biol Macromol
December 2023
School of Chemistry and Chemical Engineering, University of South China, Hengyang 421001, China; Laboratory of Protein Structure and Function, University of South China, Hengyang 421001, China. Electronic address:
Nonenzymatic glycation and the subsequent accumulation of advanced glycation end-products (AGEs) in proteins are factors underlying long-term pathogenesis in diabetes. The study of protein glycation is crucial for elucidating their relationship with diabetes mellitus and related disorders. This study explores the interaction between d-ribose and human myoglobin (HMb), as well as the protective effect of thymoquinone (TQ) on glycation.
View Article and Find Full Text PDFMedicina (Kaunas)
December 2022
Department of Life Sciences, University of Mumbai, Mumbai 400098, India.
Glycation and oxidative stress are the major contributing factors responsible for diabetes and its secondary complications. Aminoguanidine, a hydrazine derivative, is the only approved drug that reduces glycation with its known side effects. As a result, research into medicinal plants with antioxidant and antiglycation properties is beneficial in treating diabetes and its consequences.
View Article and Find Full Text PDFOxid Med Cell Longev
February 2022
IIRC-5, Clinical Biochemistry and Natural Product Research Lab, Department of Biosciences, Integral University, Lucknow, 226026 U.P., India.
The current study is aimed at studying the inhibitory effect of glycyrrhizic acid (GA) on D-ribose-mediated protein glycation via various physicochemical analyses and in silico approaches. Being a potent free radical scavenger and a triterpenoid saponin, GA plays a vital role in diminishing the oxidative stress and thus could be an effective inhibitor of the nonenzymatic glycation process. Our data showed that varying concentrations of GA inhibited the BSA-AGEs via inhibiting the formation of fructosamines, fluorescent AGEs, scavenging protein carbonyl and hydroxymethyl furfural (HMF) content, and protection against D-ribose-induced modification of BSA as evident by increased free Arg and Lys residues in GA-treated Gly-BSA samples.
View Article and Find Full Text PDFJ Biomol Struct Dyn
September 2021
IIRC-1, Laboratory of Glycation Biology and Metabolic Disorder, Department of Biosciences, Faculty of Sciences, Integral University, Lucknow, Uttar Pradesh, India.
Plasma proteins persistently bear non-enzymatic post-translational modifications (NEPTM) that proceeds with nucleophilic addition between free amino groups of proteins, and carbonyl group of reducing sugars. Glycation, a prevalent NEPTM rush by the high availability of reducing sugars results in the generation of advanced glycation end products (AGEs). Plasma proteins are more vulnerable to glycation because of the presence of multiple glycation sites and are widely studied.
View Article and Find Full Text PDFArch Biochem Biophys
June 2020
IIRC-5, Clinical Biochemistry & Natural Product Research Lab, Department of Biosciences, Integral University, Lucknow, 226026, U.P, India. Electronic address:
Non-enzymatic protein glycation results in the formation of advanced glycation end products (AGEs) leads to the pathogenesis of long-term diabetic complications. Iridin (ID), an antioxidant, plays an important role in protecting against oxidative stress and could therefore be an efficacious anti-glycating regimen. Herein, we assessed the anti-glycating potential of ID against d-ribose induced glycation of bovine serum albumin (BSA) by various biophysical and biochemical techniques.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!