Title

Polarization Independent Blue-Phase Liquid Crystal Cylindrical Lens With A Resistive Film

Keywords

atomic force microscopy; functionalization; Graphene; infrared spectroscopy; molecular dynamics simulation; phage displayed peptides; Raman spectroscopy

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. © 2012 American Chemical Society.

Publication Date

5-10-2012

Publication Title

Applied Optics

Volume

51

Issue

5

Number of Pages

2568-2572

Document Type

Article

Personal Identifier

scopus

DOI Link

https://doi.org/10.1364/AO.51.002568

Socpus ID

84861403604 (Scopus)

Source API URL

https://api.elsevier.com/content/abstract/scopus_id/84861403604

This document is currently not available here.

Share

COinS