Structure of a Peptide Adsorbed on Graphene and Graphite
Abbreviated Journal Title
Graphene; functionalization; phage displayed peptides; atomic force; microscopy; Raman spectroscopy; infrared spectroscopy; molecular; dynamics simulation; TRANSFORM INFRARED-SPECTROSCOPY; SECONDARY STRUCTURE; MEMBRANE-PROTEINS; SIMULATION; HELIX; Chemistry, Multidisciplinary; Chemistry, Physical; Nanoscience &; Nanotechnology; Materials Science, Multidisciplinary; Physics, Applied; Physics, Condensed Matter
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.
"Structure of a Peptide Adsorbed on Graphene and Graphite" (2012). Faculty Bibliography 2010s. 2840.