What is it about?
Variations in AAs self-assembly affect not only protein structures and functions, but their non-covalent interactions yield versatile assemblies vital in bio-inspired material fabrication. This study examines how Non-thermal, or Cold Atmospheric Plasma (CAP) affects tyrosine assemblies, aiming to create new biomaterial structures that could be useful for designing advanced functional materials in the future.
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Why is it important?
To understand this mechanism, this study compares different treatment times, types of gases used, and the role of acidic solutions using various testing methods to understand how this happens. Mass spectrometry showed that CAP added oxygen and nitrogen groups to tyrosine. Electron microscope images revealed larger structures and new nanomaterial forms after CAP treatment.
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This page is a summary of: Non-thermal plasma modulated l-tyrosine self-assemblies: a potential avenue for fabrication of supramolecular self-assembled biomaterials, RSC Advances, January 2024, Royal Society of Chemistry,
DOI: 10.1039/d4ra01891e.
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