Abstract
In recent years, the ability of peptides to recognize and bind to target materials have been of interest due to its tunability and selectivity. Studies have demonstrated the biorecognition capability of the peptides to bind to materials with high efficiency. Additionally, modifications to the peptides can alter the binding affinity and adsorbed structure. Chapter 1 describes the methods used for the identification and confirmation of non-naturally occurring peptide sequences with an affinity to a target material. In chapter 2, the binding affinity of three peptides, BP1, BP7 and P1, onto graphene and hexagonal boron nitride (h-BN) were observed and quantified via quartz crystal microbalance (QCM). Chapter 3 observed changes in the binding affinity and adsorbed structure on h-BN when BP7 was mutated and modified with the addition of a 10-carbon fatty acid domain. In chapter 4, the binding affinity and adsorbed overlayer on the h-BN surface was monitored when the number of carbons on the fatty acid domain on BP7 was varied. The synthesis and binding affinity of a bifunctional molecule containing two material-specific peptides was studied on graphene and h-BN in chapter 5. This bifunctional molecule was then altered to change the order of the peptides creating 3 variants in chapter 6. The binding affinity onto graphene and the ability to exfoliate graphite into graphene sheets were also analyzed in chapter 6. Taken together, this work identifies material-specific peptides and their ability to bind to both graphene and h-BN. Various modifications of the peptides have shown an enhancement of binding and changes to the adsorbed structure on the surface enabling the fabrication of a bifunctional molecule with an ability to recognize, exfoliate and assembly 2D graphene sheets.