Adsorption of Amino Acids on Graphene: Assessment of Current Force Fields
| Autor: | Siva Dasetty, Sapna Sarupria, John K. Barrows |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
chemistry.chemical_classification
education.field_of_study Chemistry Graphene Population 02 engineering and technology General Chemistry Relative strength 010402 general chemistry 021001 nanoscience & nanotechnology Condensed Matter Physics 01 natural sciences Force field (chemistry) 0104 chemical sciences law.invention Amino acid Adsorption Chemical physics law Cluster (physics) Free energies 0210 nano-technology education |
| DOI: | 10.26434/chemrxiv.7640489.v1 |
| Popis: | We compare the free energies of adsorption (∆Aads) and the structural preferences of amino acids obtained using the force fields — Amberff99SB-ILDN/TIP3P, CHARMM36/modified-TIP3P, OPLS-AA/M/TIP3P, and Amber03w/TIP4P/2005. The amino acid–graphene interactions are favorable irrespective of the force field. While the magnitudes of ∆Aads differ between the force fields, the trends in the free energy of adsorption with amino acids are similar across the studied force fields. ∆Aads positively correlates with amino acid–graphene and negatively correlates with graphene–water interaction energies. Using a combination of principal component analysis and density-based clustering technique, we grouped the structures observed in the graphene adsorbed state. The resulting population of clusters, and the conformation in each cluster indicate that the structures of the amino acid in the graphene adsorbed state vary across force fields. The differences in the conformations of amino acids are more severe in the graphene adsorbed state compared to the bulk state for all the force fields. Our findings suggest that while the thermodynamics of adsorption of proteins and peptides would be described consistently across different force fields, the structural preferences of peptides and proteins on graphene will be force field dependent. |
| Databáze: | OpenAIRE |
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