Human serum albumin interaction, in silico and anticancer evaluation of pine-gold nanoparticles

Abstract Unique characteristics displayed by phytoconstituent conjugated nanoparticles and their crucial interactions with proteins serve to develop nanoparticle-bio-interface platform. Gold nanoparticles (AuNPs) of 16 nm in size were generated using aqueous extracts of pine park (PB) and further complexed with human serum albumin (HSA). The AuNPs-protein complex was characterized by surface plasmon resonance, UV-visible and emission spectroscopy techniques. Further characterized for surface morphology and elemental composition (SEM-EDX), crystallographic quality (XRD), nanoparticles size and shape (TEM), stability (DLS), structural determination (FT-IR, and NMR) and the identification of capping agent (GC-MS). Moreover, the interaction of AuNPs with HSA was investigated using conventional spectroscopy techniques. Fluorescence quenching and absorption studies demonstrated an effective binding of HSA with oleamide capped AuNPs. The molecular docking study showed a binding affinity of -6.1 kcal/mol whereas the molecular dynamics simulation indicated that the binding of oleamide to HSA decreases the RMSD. A biological evaluation of pine bark-AuNPs showed cytotoxicity with increased cell mortality in lung cancer (A549) cells and minimal toxicity on non-cancerous human embryonic kidney (HEK293) cells.