Interaction of proteins with graphene sheet is crucial to study the exfoliation mechanism of graphene by proteins as well as to use graphene for biological applications. In this present study, we have computationally explored the interaction of a number of amino acids with the graphene sheet by employing Density Functional Theory (DFT). Counterpoise binding calculations under DFT was used to calculate the binding energies of different amino acids. The results indicate that positively charged amino acids bind better to the neutral graphene sheet in the gas phase in comparison to negatively charged amino acids. These observations are consistent with the experimental results where the logarithm of the association constant (K<sub>a</sub>), determined from Surface Plasmon measurements, can be linearly correlated to the isoelectric points of various proteins. We have also observed that polarization of graphene sheet and different charged amino acids after the optimization of these structures. The neutral amino acids, on the other hand, show no polarization and hence the binding energy is low for them.

Computational study of mechanism of different amino acids binding to Graphene sheet in gas phase with DFT

2019 Fall National Meeting

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