ArticlePloS one2019
Prevention of haemoglobin glycation by acetylsalicylic acid (ASA): A new view on old mechanism.
Article in PloS one, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 19 citations in OpenAlex.
- Unveiling the anti-glycation properties of acetylsalicylic acid: targeted inhibition of albumin glycation.Amino acids · 2026Article
- Association Between Low-Dose Aspirin Use and Early Renal Injury Biomarkers in Patients with Type 2 Diabetes Mellitus: A Retrospective Matched Cohort Study.Diabetes, metabolic syndrome and obesity : targets and therapy · 2026Article
- Unravelling the role of natural herbs for the management of diabetes mellitus.Diabetology & metabolic syndrome · 2025Review
- Glycation of Proteins and Its End Products: From Initiation to Natural Product-Based Therapeutic Preventions.ACS pharmacology & translational science · 2025Review
- Antidiabetic, hypolipidemic, and antioxidative properties of aqueous and ethanolic extracts of Sage (Veterinary world · 2025Article
- Acetylsalicylic acid disrupts SARS-CoV-2 spike protein glycosylation and selectively impairs binding to ACE2.Frontiers in immunology · 2025Article
- Antidiabetic Potential of Commonly Available Fruit Plants in Bangladesh: Updates on Prospective Phytochemicals and Their Reported MoAs.Molecules (Basel, Switzerland) · 2022Review
- Antidiabetic Phytochemicals From Medicinal Plants: Prospective Candidates for New Drug Discovery and Development.Frontiers in endocrinology · 2022Review
- Association of Novel Advanced Glycation End-Product (AGE10) with Complications of Diabetes as Measured by Enzyme-Linked Immunosorbent Assay.Journal of clinical medicine · 2021Article
- Identification of the Protein Glycation Sites in Human Myoglobin as Rapidly Induced by d-Ribose.Molecules (Basel, Switzerland) · 2021Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Diabetic hyperglycemia provokes glycation of haemoglobin (Hb), an abundant protein in red blood cells (RBCs), by increasing its exposure to carbohydrates. Acetylsalicylic acid (ASA; Aspirin) is one of the first agents, which its antiglycation effect was witnessed. Although the precise molecular mechanism of action of ASA on protein glycation is not indisputably perceived, acetylation as its main molecular mechanism has been proposed. This report aims to unravel the meticulous mechanism of action of ASA by using two ASA analogues; benzoic acid (BA) and para-nitrobenzoic acid (NBA), despite their lack of acetyl group. In this regard, the inhibitory effect of these two chemicals in comparison with ASA on Hb fructation is reported. UV-visible spectroscopy, intrinsic advanced glycation end products (AGE) fluorescence spectroscopy, extrinsic thioflavin T (ThT) binding fluorescence spectroscopy, 2,4,6-trinitrobenzenesulfonic acid (TNBSA) assay, and single cell gel electrophoresis (SCGE) were used to explore the effects of BA and NBA in comparison with aforementioned chemicals in the context of protein glycation. In spite of the lack of acetyl substitution, NBA is reported as a novel agent with prominent inhibitory efficacy than ASA on the protein glycation. This fact brings up a possible new mechanism of action of ASA and reconsiders acetylation as the sole mechanism of inhibition of protein glycation.
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