From micellar aggregates to fibrils: cold atmospheric plasma-driven structural transformation of native and glycated soluble elastin derivative.

Elastin is a key structural protein that provides elasticity to connective tissues, enabling them to stretch and recoil during normal physiological movements. It is essential for the proper functioning of mechanically active organs such as the skin, lungs, and major blood vessels. Glycation of elastin, a non-enzymatic reaction between amino acids and sugars, leads to the formation of various advanced glycation end products (AGEs), which increase tissue stiffness, reduce elasticity, and impair overall resilience. These changes contribute significantly to aging-related effects, including wrinkling and compromised structural integrity. Cold Atmospheric Plasma (CAP) has recently emerged as a versatile biomedical technology with applications ranging from biomolecule modification and surface decontamination to wound healing, sterilization, and cancer therapy. In this study, we examined the interaction of CAP with both native and glycated soluble elastin derivative (SED) to understand CAP-induced structural modifications and alterations in self-assembly behavior. Microscopy revealed that CAP treatment facilitated the formation of long fibrillar structures in native SED. In contrast, CAP exposure, particularly at the 7 minute mark, led to noticeable fragmentation of AGEs in glycated SED. Circular dichroism (CD) spectroscopy showed significant changes in secondary structure, and FTIR analysis confirmed modifications in functional groups across both sample types. Overall, these findings enhance our understanding of CAP-protein interactions and highlight its potential in biomaterials development, therapeutic applications, and studies of protein modification in disease contexts.