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Peptide conjugate molecules comprising a gold-binding peptide (e.g., AYSSGAPPMPPF) attached to an aliphatic tail have proven to be powerful agents for directing the synthesis and assembly of gold nanoparticle superstructures, in particular chiral helices having interesting plasmonic chiroptical properties. The composition and structure of these molecular agents can be tailored to carefully tune the structure and properties of gold nanoparticle single and double helices. To date, modifications to the β-sheet region (AYSSGA) of the peptide sequence have not been exploited to control the metrics and assembly of such superstructures. We report here that systematic peptide sequence variation in a series of gold-binding peptide conjugate molecules can be leveraged not only to affect the assembly of peptide conjugates but also to control the synthesis, assembly, and optical properties of gold nanoparticle superstructures. Depending upon the hydrophobicity of a single-amino acid variant, the conjugates yield either dispersed gold nanoparticles or helical superstructures. These results provide evidence that subtle changes to peptide sequence, via single-amino acid variation in the β-sheet region, can be leveraged to program structural control in chiral gold nanoparticle superstructures.
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Developing a rational approach to designing recombinant proteins for peptide-directed nanoparticle synthesis
The controlled formation of nanoparticles with optimum characteristics and functional aspects has proven successful via peptide-mediated nanoparticle synthesis. However, the effects of the peptide sequence and binding motif on surface features and physicochemical properties of nanoparticles are not well-understood. In this study, we investigate in a comparative manner how a specific peptide known as Pd4 and its two known variants may form nanoparticles both in an isolated state and when attached to a green fluorescent protein (GFPuv). More importantly, we introduce a novel computational approach to predict the trend of the size and activity of the peptide-directed nanoparticles by estimating the binding affinity of the peptide to a single ion. We used molecular dynamics (MD) simulations to explore the differential behavior of the isolated and GFP-fused peptides and their mutants. Our computed palladium (Pd) binding free energies match the typical nanoparticle sizes reported from transmission electron microscope pictures. Stille coupling and Suzuki–Miyaura reaction turnover frequencies (TOFs) also correspond with computationally predicted Pd binding affinities. The results show that while using Pd4 and its two known variants (A6 and A11) in isolation produces nanoparticles of varying sizes, fusing these peptides to the GFPuv protein produces nanoparticles of similar sizes and activity. In other words, GFPuv reduces the sensitivity of the nanoparticles to the peptide sequence. This study provides a computational framework for designing free and protein-attached peptides that helps in the synthesis of nanoparticles with well-regulated properties.
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- Award ID(s):
- 1945465
- PAR ID:
- 10399304
- Date Published:
- Journal Name:
- Nanoscale Advances
- Volume:
- 4
- Issue:
- 15
- ISSN:
- 2516-0230
- Page Range / eLocation ID:
- 3161 to 3171
- Format(s):
- Medium: X
- Sponsoring Org:
- National Science Foundation
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- Free Publicly Accessible Full Text
-
Accepted Manuscript1.0
- Journal Article:
- https://doi.org/10.1039/D2NA00212D
