Prunin from Poncirus trifoliata (L.) Rafin Inhibits Aldose Reductase and Glucose-Fructose-Mediated Protein Glycation and Oxidation of Human Serum Albumin.
Md Yousof AliGerald W. ZamponiQudeer Ahmed AbdulSu Hui SeongByung-Sun MinHyun Ah JungJae-Sue ChoiPublished in: Journal of agricultural and food chemistry (2024)
Diabetes complications are associated with aldose reductase (AR) and advanced glycation end products (AGEs). Using bioassay-guided isolation by column chromatography, 10 flavonoids and one coumarin were isolated from Poncirus trifoliata Rafin and tested in vitro for an inhibitory effect against human recombinant AR (HRAR) and rat lens AR (RLAR). Prunin, narirutin, and naringin inhibited RLAR (IC 50 0.48-2.84 μM) and HRAR (IC 50 0.68-4.88 μM). Docking simulations predicted negative binding energies and interactions with the RLAR and HRAR binding pocket residues. Prunin (0.1 and 12.5 μM) prevented the formation of fluorescent AGEs and nonfluorescent N ε -(carboxymethyl) lysine (CML), as well as the fructose-glucose-mediated protein glycation and oxidation of human serum albumin (HSA). Prunin suppressed the formation of the β-cross-amyloid structure of HSA. These results indicate that prunin inhibits oxidation-dependent protein damage, AGE formation, and AR, which may help prevent diabetes complications.
Keyphrases
- human serum albumin
- protein protein
- type diabetes
- binding protein
- cardiovascular disease
- hydrogen peroxide
- amino acid
- endothelial cells
- molecular dynamics
- risk factors
- mass spectrometry
- small molecule
- blood pressure
- quantum dots
- dna binding
- nitric oxide
- metabolic syndrome
- skeletal muscle
- transcription factor
- fluorescent probe
- pluripotent stem cells
- simultaneous determination