Tailoring Peptide Self-Assembly and Formation of 2D Nanoribbons on Mica and HOPG Surface

Abstract

Studying the interactions between biomolecules and material interfaces play a crucial role in the designing and synthesizing of functional bionanomaterials with tailored structure and function. Previously, a lot of studies were performed on the self-assembly of peptides in solution through internal and external stimulations, which mediated the creation of peptide nanostructures from zero-dimension to three-dimension. In this study, we demonstrate the self-assembly behavior of the GNNQQNY peptide on the surface of mica and highly oriented pyrolytic graphite through tailoring the self-assembly conditions. Various factors, such as the type of dissolvent, peptide concentration, pH value, and evaporation period on the formation of peptide nanofibers and nanoribbons with single- and bi-directional arrays are investigated. It is found that the creation of peptide nanoribbons on both mica and HOPG can be achieved effectively through adjusting and optimizing the experimental parameters. Based on the obtained results, the self-assembly and formation mechanisms of peptide nanoribbons on both material interfaces are discussed. It is expected that the findings obtained in this study will inspire the design of motif-specific peptides with high binding affinity towards materials and mediate the green synthesis of peptide-based bionanomaterials with unique function and application potential.

Two-Dimensional Layered Nanomaterials Steering Self-Assembly of Dodecapeptides with Three Building Blocks

“…The third point concerns the limited technique allowing us to obtain details on the growth dynamics of peptide self-assembly in molecular native structures needing a fast scanning, e.g., imaging rate 1 s per frame (s/f) or even less, and molecular resolution structures, e.g., 1 nm resolution comparable to peptide sizes, of the repeated unit cells. It is known that the self-assembly of peptides on solids took place in aqueous solution; most of the work in literature ,,− has shown the morphologies and structures captured by ex-situ atomic force microscopy (AFM) imaging in a dry condition. The in-situ AFM allowed to reveal the native single-peptide molecular structures under physiological conditions, which was often destructed in a drying sample used for ex - situ AFM measurements.…”