Journal
NANO LETTERS
Volume 12, Issue 5, Pages 2342-2346Publisher
AMER CHEMICAL SOC
DOI: 10.1021/nl300286k
Keywords
Graphene; functionalization; phage displayed peptides; atomic force microscopy; Raman spectroscopy; infrared spectroscopy; molecular dynamics simulation
Categories
Funding
- National Science Foundation [0955625]
- Air Force Office of Scientific Research
- Direct For Mathematical & Physical Scien
- Division Of Materials Research [0955625] Funding Source: National Science Foundation
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Noncovalent functionalization of graphene using peptides is a promising method for producing novel sensors with high sensitivity and selectivity. Here we perform atomic force microscopy, Raman spectroscopy, infrared spectroscopy, and molecular dynamics simulations to investigate peptide-binding behavior to graphene and graphite. We studied a dodecamer peptide identified with phage display to possess affinity for graphite. Optical spectroscopy reveals that the peptide forms secondary structures both in powder form and in an aqueous medium. The dominant structure in the powder form is a-helix, which undergoes a transition to a distorted helical structure in aqueous solution. The peptide forms a complex reticular structure upon adsorption on graphene and graphite, having a helical conformation different from alpha-helix due to its interaction with the surface. Our observation is consistent with our molecular dynamics calculations, and our study paves the way for rational functionalization of graphene using biomolecules with defined structures and, therefore, functionalities.
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