title: Peptide interfaces with graphene: an emerging intersection of analytical chemistry, theory, and materials.
abstract: Because noncovalent interface functionalization is frequently required in graphene-based devices, biomolecular self-assembly has begun to emerge as a route for controlling substrate electronic structure or binding specificity for soluble analytes. The remarkable diversity of structures that arise in biological self-assembly hints at the possibility of equally diverse and well-controlled surface chemistry at graphene interfaces. However, predicting and analyzing adsorbed monolayer structures at such interfaces raises substantial experimental and theoretical challenges. In contrast with the relatively well-developed monolayer chemistry and characterization methods applied at coinage metal surfaces, monolayers on graphene are both less robust and more structurally complex, levying more stringent requirements on characterization techniques. Theory presents opportunities to understand early binding events that lay the groundwork for full monolayer structure. However, predicting interactions between complex biomolecules, solvent, and substrate is necessitating a suite of new force fields and algorithms to assess likely binding configurations, solvent effects, and modulations to substrate electronic properties. This article briefly discusses emerging analytical and theoretical methods used to develop a rigorous chemical understanding of the self-assembly of peptide-graphene interfaces and prospects for future advances in the field.
authors.affiliation: Department of Chemistry, Purdue University, West Lafayette, IN, 47907, USA.
authors.forename: Shane R
authors.initials: SR
authors.lastname: Russell
authors.affiliation: Department of Chemistry, Purdue University, West Lafayette, IN, 47907, USA. claridge@purdue.edu.|Weldon School of Biomedical Engineering, Purdue University, West Lafayette, IN, 47907, USA. claridge@purdue.edu.
authors.forename: Shelley A
authors.initials: SA
authors.lastname: Claridge
mesh_terms: D006108:Graphite / Q000737:chemistry*; D018625:Microscopy, Atomic Force; D008962:Models, Theoretical; D010455:Peptides / Q000737:chemistry*; D058525:Quartz Crystal Microbalance Techniques
chemical_list: D010455:Peptides; D006108:Graphite
keywords: Atomic force microscopy; Graphene; Peptide; Polarization modulation IR reflection–absorption spectroscopy; Quartz crystal microgravimetry; Scanning tunneling microscopy