Biophysical Insights into Phycocyanin Binding and Antiglycation Activity with Bovine Serum Albumin

Journal Article

2025

Background & Objectives: Protein glycation results in advanced glycation end-products (AGEs), contributing to degenerative diseases. Phycocyanin (PC), a natural antioxidant, has potential to reduce glycation-induced damage. This study evaluates the binding interaction of PC with bovine serum albumin (BSA), its antiglycation efficacy, and associated thermodynamic properties. Methods: BSA at a concentration of 0.3 mg/mL was titrated with PC in the range of 0 to 50 μM. Fluorescence emission spectra between 300 and 500 nm were measured at excitation wavelength 280 nm using a spectrofluorometer with Peltier temperature control, set at 25, 30, and 37 °C. Binding constants, quenching parameters, and thermodynamic values were calculated. The antiglycation potential was evaluated by measuring protein carbonyl content, fructosamine levels, and AGE-specific fluorescence. Results: Fluorescence quenching analysis demonstrated a dynamic quenching mechanism, exhibiting increased efficiency at elevated temperatures. Binding constants confirmed a strong interaction between PC and BSA, driven by hydrophobic forces, with negative ΔG values indicating spontaneity. Antiglycation assays revealed reduced levels of protein carbonyls, fructosamine content, and AGE formation. Conclusions: PC demonstratesstrong BSA binding through hydrophobic interactions and effectively inhibits glycation-related modifications, highlightingits potential as a therapeutic agent against glycation-induced disorders.

• Publisher Name: SAGE
• Publishing City: UK
• Volume Number: 20
• Issue Number: 4
• Magazine \ Newspaper: Natural Product Communications