Peptide interactions with zigzag edges in graphene
Abstract
Recognition and manipulation of graphene edges enable the control of physical properties of graphene-based devices. Recently, the authors have identified a peptide that preferentially binds to graphene edges from a combinatorial peptide library. In this study, the authors examine the functional basis for the edge binding peptide using experimental and computational methods. The effect of amino acid substitution, sequence context, and solution pH value on the binding of the peptide to graphene has been investigated. The N-terminus glutamic acid residue plays a key role in recognizing and binding to graphene edges. The protonation, substitution, and positional context of the glutamic acid residue impact graphene edge-binding. Our findings provide insights into the binding mechanisms and the design of peptides for recognizing and functionalizing graphene edges.
Document Details
- Document Type
- Pub Defense Publication
- Publication Date
- Nov 04, 2016
- Source ID
- 10.1116/1.4966266
Entities
People
- Barry L. Farmer
- Michael McAlpine
- Rajesh R Naik
- Steve S. Kim
- Yen H. Ngo
- Zhifeng Kuang
Organizations
- 711th Human Performance Wing
- Air Force Office of Scientific Research
- Air Force Research Laboratory Materials and Manufacturing Directorate
- University of Minnesota