Structure of a Peptide Adsorbed on Graphene and Graphite

    Authors

    J. Katoch; S. N. Kim; Z. F. Kuang; B. L. Farmer; R. R. Nalk; S. A. Tatulian;M. Ishigami

    Comments

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    Abbreviated Journal Title

    Nano Lett.

    Keywords

    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

    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 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.

    Journal Title

    Nano Letters

    Volume

    12

    Issue/Number

    5

    Publication Date

    1-1-2012

    Document Type

    Article

    Language

    English

    First Page

    2342

    Last Page

    2346

    WOS Identifier

    WOS:000303696400029

    ISSN

    1530-6984

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