Non-thermal plasma modulated l-tyrosine self-assemblies: a potential avenue for fabrication of supramolecular self-assembled biomaterials.

ABSTRACT: Aromatic amino acids (AAs) have garnered particular interest due to their pivotal roles in numerous biological processes and disorders. Variations in AA self-assembly not only affect protein structures and functions, but their non-covalent interactions such as hydrogen bonding, van der Waals forces, and π-π stacking, yield versatile assemblies vital in bio-inspired material fabrication. Tyrosine (Tyr), a non-essential aromatic amino acid, holds multifaceted significance in the body as a protein building block, neurotransmitter precursor, thyroid hormone contributor, and melanin synthesis regulator. The proficiency of Cold Atmospheric Plasma (CAP) in generating a spectrum of reactive oxygen and nitrogen species has spurred innovative research avenues in the studies of biomolecular component

SUBMITTER: Bhatt P 

PROVIDER: S-EPMC11056826 | biostudies-literature | 2024 Apr

REPOSITORIES: biostudies-literature