Homeopathic Formulations of Syzygium jambolanum Alleviate Glycation-Mediated Structural and Functional Modifications of Albumin: Evaluation through Multi-Spectroscopic and Microscopic Approaches.

Background: The growing interest in identifying the mode of action of traditional medicines has strengthened its research. () is commonly prescribed in homeopathy and is a rich source of phytochemicals.

Objective: The present study aims to shed light on the anti-glycation molecular mechanism of mother tincture (MT), 30c, and 200c on glycated human serum albumin (HSA) by multi-spectroscopic and microscopic approaches.

Methods: The phytochemicals and antioxidant potential of the formulations were estimated by the high-performance liquid chromatography and spectroscopic technique, respectively. Glycation was initiated by incubating HSA with methylglyoxal, three formulations, and the known inhibitor aminoguanidine in separate tubes at 37°C for 48 hours. The formation of glycation adducts was assessed by spectrofluorometer and affinity chromatography. The structural modifications were analyzed through circular dichroism, Fourier transform infrared spectroscopy, turbidity, 8-anilinonapthalene-1-sulfonic acid fluorescence, and nuclear magnetic resonance. Further, the formation of the aggregates was examined by thioflavin T, native-polyacrylamide gel electrophoresis, and transmission electron microscopy. Additionally, the functional modifications of glycated HSA were determined by esterase-like activity and antioxidant capacity. The binding analysis of formulations with glycated HSA was evaluated by surface plasmon resonance (SPR).

Results: formulations MT, 30c, and 200c contained gallic acid and ellagic acid as major phytochemicals, with concentrations of 16.02, 0.86, and 0.52 µg/mL, and 227.35, 1.35, and 0.84 µg/mL, respectively. Additionally, all three formulations had remarkable radical scavenging ability and could significantly inhibit glycation compared with aminoguanidine. Further, formulations inhibited albumin's structural and functional modifications. SPR data showed that formulations bind to glycated HSA with an equilibrium dissociation constant of 1.10 nM.

Conclusion: formulations inhibited the glycation process while maintaining the structural and functional integrity of HSA.