Structure of a Peptide Adsorbed on Graphene and Graphite

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 beha...

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Bibliographic Details
Published in:Nano letters 2012-05, Vol.12 (5), p.2342-2346
Main Authors: Katoch, Jyoti, Kim, Sang Nyon, Kuang, Zhifeng, Farmer, Barry L, Naik, Rajesh R, Tatulian, Suren A, Ishigami, Masa
Format: Article
Language:English
Subjects:
Adsorption
Atomic structure
Biomolecules
Cross-disciplinary physics: materials science
rheology
Exact sciences and technology
Fullerenes and related materials
diamonds, graphite
General equipment and techniques
Graphene
Graphite
Graphite - chemistry
Helical
Instruments, apparatus, components and techniques common to several branches of physics and astronomy
Materials science
Microscopy, Atomic Force
Molecular dynamics
Molecular structure
Peptides
Peptides - chemistry
Physics
Protein Conformation
Sensors (chemical, optical, electrical, movement, gas, etc.)
remote sensing
Specific materials
Surface chemistry
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Summary: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 α-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 α-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.
ISSN:1530-6984
1530-6992
DOI:10.1021/nl300286k