Exploring impact of cold atmospheric plasma directed self-assembly of glycated bovine serum albumin

Bovine Serum Albumin (BSA) is a globular, water-soluble protein widely used as a model system due to its stability, binding capacity, and structural similarity to human serum albumin (HSA). Cold atmospheric plasma (CAP) has emerged as a versatile tool for biomolecule modification, sterilization, food preservation, and wound healing. This study explores the effects of CAP on glycated BSA, focusing on structural and self-assembly processes. SEM analysis reveals that CAP induces distinct protein self-assemblies depending on treatment duration. Thioflavin assays show increased fluorescence intensity in CAP-treated glycated BSA compared to native and glycated BSA, indicating an enhancement in β-sheet content and self-assembly. These findings offer valuable insights into CAP's role in modulating protein structures, with implications for biomaterials, disease mechanisms, and protein engineering.