ArticleAmino acids2026
Unveiling the anti-glycation properties of acetylsalicylic acid: targeted inhibition of albumin glycation.
Article in Amino acids, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Abstract
Glycation due to increased blood sugar levels aggravates diabetic complications. Glycation hampers the structural and functional integrity of human serum albumin (HSA). Acetylsalicylic acid (ASA)/aspirin exhibits anti-glycation properties. Although the precise molecular mechanism of ASA in glycation has not yet been conclusively demonstrated, acetylation has been considered the central mechanism underlying its biological action. The present study aims to unveil the specific mechanism of action of ASA on glycated HSA through meticulously designed approaches. Fluorescence and UV-visible spectroscopy were used to analyse glycation adducts in the presence of ASA. ANS-based fluorescence spectroscopy, sodium dodecyl sulfate polyacrylamide gel electrophoresis, Fourier transform infrared spectroscopy, field-emission scanning electron microscopy, and high-performance liquid chromatography were used to study the structural modifications of glycated HSA in the presence of ASA. Furthermore, we investigated functional modifications in glycated HSA using nuclear magnetic resonance spectroscopy. The analyzed data showed a direct association between glycation and the impaired structural and functional integrity of HSA, which was partially restored by ASA. Our data corroborate that ASA's prominent anti-glycation activity may be attributable to mechanisms other than acetylation.
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