Interplay of Self-Assembling Aromatic Amino Acids and Functionalized Gold Nanoparticles Generating Supramolecular Structures.

In the recent years, protein metabolite-based self-assembled supramolecular structures have been linked to various pathological disorders. The self-assembly of protein over nanoparticle surfaces can lead to the formation of corona aggregates that have gained much attention owing to biomedical healthcare relevance. However, limited studies are available at the interface of amyloid formation and nanoparticle surfaces. In this context, the present study demonstrated the effect of specifically functionalized gold nanoparticles on the potential amyloid formation by self-assembled aromatic amino acids. The coassembly of aromatic amino acids and gold nanoparticles was utilized to gain mechanistic insight into altered intermolecular interactions between amino acid monomers. The polymorphism, thermal stability, and morphological pattern of coassembled aromatic amino acids and gold nanoparticle (Co-AA:AuNP) structures were analyzed using X-ray diffraction, thermogravimetric analysis, and field emission scanning electron microscopy, respectively. Finally, amyloid like aggregation of Co-AA:AuNP structures were evaluated using thioflavin T fluorescence assay in solution as well as the deposited phase. The present work is crucial for the design and usage of nanoparticles in biomedical applications, which may trigger amyloid-like metabolite aggregation leading to pathological disorders.