The interactions of N- and C- terminal peptides of bovine serum albumin (BSA) and graphene bilayers were studied by molecular dynamics (MD) simulations. Each of the peptides were 15 residues in length and were prepared in Maestro/Schrodinger suites, along with a 25x25 graphene bilayer with zigzag and armchair edges. The N- and C- termini on the non-interacting ends in each peptide were blocked by amidation and acetylation. Once the initial nanosheet-peptide system was built, a water box of dimensions 150 x 120 x 60 Å<sup>3</sup> filled with TIP3P water molecules was built so that the graphene bilayer and peptide fit comfortably inside the water box. The system was minimized with OLPS_2005 and the simulations were run for a total of 50 ns with no restraints. Analysis of final conformations of the peptides on the graphene sheet showed that both the N- and C- termini strongly interacted with the corner edges of the graphene, establishing that the edge of the graphene sheet has a higher affinity for biomolecules rather than the basal planes. Due to the charge on both termini, specifically the +1 charge on the free N- terminus and the -1 charge on the free C- terminus, polarity of the graphene bilayer appears to be the key to rationalize the observed interactions.

Interactions between N- and C- terminal peptides of serum albumin and graphene bilayers using molecular dynamic simulations

ACS Spring 2022

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