Akademik Veri Yönetim Sistemi
8th International Conference on Advances in Natural and Applied Sciences (ICANAS 2025), Antalya, Türkiye, 28 - 31 Ekim 2025, ss.199, (Özet Bildiri)
Food additives are widely used to extend shelf life, enhance visual appeal, and influence consumer preferences. Among them, E102 (tartrazine), a synthetic azo dye, is commonly applied as a colorant in beverages, confectionery, and processed foods [1]. However, debates persist regarding its potential to cause allergic reactions, behavioral disorders, and metabolic effects. Thus, understanding the biological impact of food additives is crucial for public health. In recent years, research on the interactions of food dyes with human protein targets has rapidly increased. In this context, target fishing studies, followed by molecular docking, provides a robust approach [2]. This study investigates potential human protein targets of tartrazine and its interactions using in silico docking methods. The structure of tartrazine (CID: 164825) was retrieved from PubChem. Target fishing with SwissTargetPrediction identified Beta-lactamase (1A8T), Glycogen synthase kinase-3 beta (1PYX), Carbonic anhydrase 4 (5KU6), and Aldo-keto reductase family 1 member C1 (1MRQ) as the most reliable targets. Ligand minimization was performed using LigPrep in Schrödinger Maestro, while receptor structures were obtained from the RCSB Protein Data Bank and prepared with the Protein Preparation tool. Docking and visualization were carried out in Schrödinger Maestro (v13.9.138). Docking results showed strong binding affinities: tartrazine–Beta-lactamase (-10.145 kcal/mol), tartrazine–Glycogen synthase kinase-3 beta (-9.803 kcal/mol), tartrazine–Carbonic anhydrase 4 (-9.281 kcal/mol), and tartrazine–Aldo-keto reductase family 1 member C1 (-8.508 kcal/mol). These findings suggest tartrazine may provide valuable insights into potential protein targets for use safety research.