title: Structure of a peptide adsorbed on graphene and graphite.
abstract: 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.
authors.affiliation: Department of Physics, University of Central Florida, Orlando, Florida 32816-2385, USA.
authors.forename: Jyoti
authors.initials: J
authors.lastname: Katoch
authors.forename: Sang Nyon
authors.initials: SN
authors.lastname: Kim
authors.forename: Zhifeng
authors.initials: Z
authors.lastname: Kuang
authors.forename: Barry L
authors.initials: BL
authors.lastname: Farmer
authors.forename: Rajesh R
authors.initials: RR
authors.lastname: Naik
authors.forename: Suren A
authors.initials: SA
authors.lastname: Tatulian
authors.forename: Masa
authors.initials: M
authors.lastname: Ishigami
mesh_terms: D000327:Adsorption; D006108:Graphite / Q000737:chemistry*; D018625:Microscopy, Atomic Force; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation
chemical_list: D010455:Peptides; D006108:Graphite