Interaction between peptides and an MoS2 monolayer containing a nanopore: First-principles calculations

Abstract

• The reaction between small peptide molecules and the MoS2 nanopore are explored: • Serine and Glycylglycine don't have any bonding and interaction with MoS2/NP. Each plays the role of a passer in the system. • Two dipeptides, Aspartame and Carnosine, and the tripeptide Glutathione react with Mo and S atoms surrounding the hole and form stable compounds. First-principles density functional theory (DFT) is employed to explore the interaction between a peptide molecule and two-dimensional (2-D) monolayer of molybdenum disulfide (MoS 2 ) containing a nanopore. A variety of monopeptides, dipeptides and also a tripeptide are individually positioned in the hole of a MoS 2 layer and the overall electronic structure calculated. The results indicate that bonding occurs between some molecules and the hole edge. The outcome of reaction can be predicted through the potential energy surface. These results strongly suggest that 2-D MoS 2 nanopores have a wide range of biological applications and deserve further exploitation by experiment.