Adsorption and Conformational Evolution of Alpha-Helical BSA Segments on Graphene: A Molecular Dynamics Study

Abstract

Molecular dynamics (MD) simulations are performed to investigate the adsorption mechanics and conformational dynamics of single and multiple bovine serum albumin (BSA) peptide segments on single-layer graphene through analysis of parameters such as the root-mean-square displacements, number of hydrogen bonds, helical content, interaction energies, and motions of mass center of the peptides. It is found that for the single segment system, destabilization of the helical structures in the form of the reduction in hydrogen bond numbers and α-helical content of the peptides occurred due to the strong interactions between BSA peptides and graphene. Similar destabilizations of the individual segments in the multi-segment system can occur as well, albeit with greater complexity and in a lesser degree due to the inter-segment interactions. Alleviation of decreases in the total helical content in the multi-segment system indicates protective capabilities of segment-segment interactions, which weaken their interactions with graphene. Diffusive motion upon adsorption of the segment(s) onto graphene is found to be highly confined, and the distance traversed by each segment in the multi-segment system was more significant than that in the single segment system, similarly attributable to reductions in their interactions with graphene due to inter-segment interactions.

Interfacing Graphene-Based Materials With Neural Cells

“…In 2016, Yeo et al ( 2016 ) investigated the adsorption mechanism of single and multiple bovine serum albumin (BSA) peptide segments on G, through the analysis of a broad set of parameters such as root-mean-square displacement, number of hydrogen bonds, helical content, interaction energies, and peptide center-of-mass displacement. The authors observed a destabilization of the helical structures in the single segment system, due to strong interactions between the peptide and the substrate.…”

Graphene oxide as a dual template for induced helicity of peptides

“…Several previous studies revealed the destruction of α-helix at the surface of graphene and GO and the formation of 3 10 helix and turn. 42–46 Zuo et al reported the adsorption of a Villin headpiece (HP35) on the surface of graphene and carbon nanotube and the loss of its native α-helix structure through strong π–π stacking interactions between graphene and aromatic residues. 47 Here, we have observed a similar strong interactions between the GO and aromatic residue positions such as Trp4, Trp8, Trp11 and Trp15 (Fig.…”

Enhanced Stability and Mechanical Properties of a Graphene–Protein Nanocomposite Film by a Facile Non-Covalent Self-Assembly Approach

“…After interactions with GO sheets, the α -helix contents of BSA and HB decreased to 14.6 and 16.4%, respectively. Our previous work has revealed the binding mechanism of the α -helix fragments of BSA with graphene by using molecular dynamics simulations [ 38 ]. The adsorption of an α -helix on the surface of graphene induces a transition from to the 3 10 -helix structure, which was reflected in the substantial increase in random coils from 24.1 to 42.2% for BSA in this work.…”