Chalcone derivatives' interaction with human serum albumin and cyclooxygenase-2

Chalcone derivatives are an extremely valuable class of compounds, primarily due to the keto-ethylenic group, CO-CH00000000000000000000000000000000111111110000000011111111000000000000000000000000CH-, they contain. Moreover, the presence of a reactive alpha,beta-unsaturated carbonyl group confers upon them a broad range of pharmacological properties. Recent developments in heterocyclic chemistry have led to the synthesis of chalcone derivatives, which have been biologically investigated for their activity against certain diseases. In this study, we investigated the binding of new chalcone derivatives with COX-2 (cyclooxygenase-2) and HSA (Human Serum Albumin) using spectroscopic and molecular modeling studies. COX-2 is commonly found in cancer and plays a role in the production of prostaglandin E (2), which can help tumors grow by binding to receptors. HSA is the most abundant protein in blood plasma, and it transports various compounds, including hormones and fatty acids. The conformation of chalcone derivatives in the HSA complex system was established through fluorescence steady and excited state spectroscopy techniques and FTIR analyses. To gain a more comprehensive understanding, molecular docking, and dynamics were conducted on the target protein (COX-2) and transport protein (HSA). In addition, we conducted density-functional theory (DFT) and single-point DFT to understand intermolecular interaction in protein active sites. In this study, various spectroscopic and computational techniques were utilized to investigate how new chalcone derivatives bind with cyclooxygenase-2 (COX-2) and Human Serum Albumin (HSA).