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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
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Interplay of Self-Assembling Aromatic Amino Acids and Functionalized Gold Nanoparticles Generating Supramolecular
Prabhjot Singh1, Nikesh Narang2, Rohit K Sharma2
1Centre for Nanoscience and Nanotechnology, Panjab University, Sector 14, Chandigarh 160014, India.
ACS Applied Bio Materials
|January 13, 2022
Summary
Gold nanoparticles influence aromatic amino acid self-assembly, potentially triggering amyloid-like aggregation. This research is vital for understanding nanoparticle safety in biomedical applications and preventing related diseases.
Area of Science:
- Biomaterials Science
- Nanotechnology
- Biochemistry
Background:
- Protein metabolite self-assembly into supramolecular structures is linked to pathological disorders.
- Protein corona formation on nanoparticles is relevant to biomedical applications.
- Limited research exists on amyloid formation at the nanoparticle-biointerface.
Purpose of the Study:
- To investigate the effect of functionalized gold nanoparticles on amyloid formation by self-assembled aromatic amino acids.
- To gain mechanistic insights into altered intermolecular interactions during coassembly.
- To assess the potential for nanoparticle-induced amyloid-like aggregation.
Main Methods:
- Coassembly of aromatic amino acids and gold nanoparticles.
- Characterization using X-ray diffraction (XRD), thermogravimetric analysis (TGA), and field emission scanning electron microscopy (FESEM).
- Thioflavin T (ThT) fluorescence assay to evaluate amyloid-like aggregation.
Main Results:
- Gold nanoparticles altered the polymorphism, thermal stability, and morphology of self-assembled aromatic amino acids.
- Coassembled aromatic amino acid and gold nanoparticle (Co-AA:AuNP) structures exhibited amyloid-like aggregation.
- Aggregation was confirmed using ThT assay in both solution and deposited phases.
Conclusions:
- Functionalized gold nanoparticles can influence amino acid self-assembly and promote amyloid-like aggregation.
- Understanding these interactions is crucial for the safe design and application of nanoparticles in biomedicine.
- This work highlights the potential risk of nanoparticles triggering pathological metabolite aggregation.

