title: Controlling the surface chemistry of graphite by engineered self-assembled peptides.
abstract: The systematic control over surface chemistry is a long-standing challenge in biomedical and nanotechnological applications for graphitic materials. As a novel approach, we utilize graphite-binding dodecapeptides that self-assemble into dense domains to form monolayer-thick long-range-ordered films on graphite. Specifically, the peptides are rationally designed through their amino acid sequences to predictably display hydrophilic and hydrophobic characteristics while maintaining their self-assembly capabilities on the solid substrate. The peptides are observed to maintain a high tolerance for sequence modification, allowing control over surface chemistry via their amino acid sequence. Furthermore, through a single-step coassembly of two differently designed peptides, we predictably and precisely tune the wettability of the resulting functionalized graphite surfaces from 44° to 83°. The modular molecular structures and predictable behavior of short peptides demonstrated here give rise to a novel platform for functionalizing graphitic materials that offers numerous advantages, including noninvasive modification of the substrate, biocompatible processing in an aqueous environment, and simple fusion with other functional biological molecules.
authors.affiliation: Materials Science and Engineering, Genetically Engineered Materials Science and Engineering Center, University of Washington, 302 Roberts Hall, Seattle, Washington 98195, USA.
authors.forename: Dmitriy
authors.initials: D
authors.lastname: Khatayevich
authors.forename: Christopher R
authors.initials: CR
authors.lastname: So
authors.forename: Yuhei
authors.initials: Y
authors.lastname: Hayamizu
authors.forename: Carolyn
authors.initials: C
authors.lastname: Gresswell
authors.forename: Mehmet
authors.initials: M
authors.lastname: Sarikaya
mesh_terms: D000595:Amino Acid Sequence; D001672:Biocompatible Materials / Q000737:chemistry*; D006108:Graphite / Q000737:chemistry*; D057927:Hydrophobic and Hydrophilic Interactions; D018625:Microscopy, Atomic Force; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D015202:Protein Engineering; D013499:Surface Properties; D014867:Water / Q000737:chemistry; D017155:Wettability
chemical_list: D001672:Biocompatible Materials; D010455:Peptides; D014867:Water; D006108:Graphite