Peptide interactions with zigzag edges in graphene.
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.
Materials and Manufacturing Directorate, Air Force Research Laboratory, WPAFB, Ohio 45433.
Zhifeng
Z
Kuang
711th Human Performance Wing, Air Force Research Lab, WPAFB, Ohio 45433.
Steve S
SS
Kim
711th Human Performance Wing, Air Force Research Lab, WPAFB, Ohio 45433.
Yen H
YH
Ngo
Department of Mechanical Engineering, University of Minnesota, Minneapolis, Minnesota 55455.
Michael C
MC
McAlpine
Materials and Manufacturing Directorate, Air Force Research Laboratory, WPAFB, Ohio 45433.
Barry L
BL
Farmer
711th Human Performance Wing, Air Force Research Lab, WPAFB, Ohio 45433.
Rajesh R
RR
Naik
D019943:Amino Acid Substitution; D019295:Computational Biology; D018698:Glutamic Acid / Q000235:genetics / Q000378:metabolism; D006108:Graphite / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D010455:Peptides / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D013499:Surface Properties
D010455:Peptides; D018698:Glutamic Acid; D006108:Graphite