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

http://dx.doi.org/10.1142/S1758825116500216Molecular 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, inter- action 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 individ- ual segments in the multi-segment system can occur as well, albeit with greater complex- ity 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 sig- nificant than that in the single segment system, similarly attributable to reductions in their interactions with graphene due to inter-segment interaction.

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