Impact of Cold Atmospheric Plasma Treatment on Native and Glycated Collagen

ABSTRACT Collagen is a major structural protein in the body, providing critical stability to the skin. Recent advancements have highlighted cold atmospheric plasma (CAP) as a versatile tool for various applications, including biomolecule modification, sterilization, food preservation, and wound healing. This study investigates the effects of CAP on both native and glycated collagen, analyzing the resulting changes. SEM and AFM analyses reveal that CAP induces protein self‐assembly in both glycated and non‐glycated collagen. Thioflavin assays further demonstrate that CAP‐treated glycated collagen exhibits greater fluorescence intensity compared to untreated glycated samples, indicating an increase in β‐sheet content and suggesting enhanced self‐assembly. These findings provide insights into the potential applications of CAP in modulating protein structures and understanding various biological processes and diseases.