Nature of Molecular Interactions of Peptides with Gold, Palladium, and Pd-Au Bimetal Surfaces in Aqueous Solution (Supporting Information)

摘要

In summary, we employ a classical atomistic molecular dynamics approach to analyze specific peptide binding to metal surfaces in comparison with thermochemical, IR, NMR, and TEM measurements. Modeling at all levels, molecular, coarse-grain, and bioinformatics, is ultimately important in identifying the most suitable peptide sequences for controlled binding and detachment. Quantum-mechanical approaches indicate approximate trends of the interaction of peptide fragments and a few solvent molecules with parts of a surface, and have shown that covalent interactions with metal surfaces are modest to small. However, such approaches cannot fully explain the mechanisms of binding due to limitations to static calculations. Coarse-grain approaches can be computationally -10(3) times more efficient and include certain specific peptide-surface interactions. A critical role can also be attributed to bioinformatics approaches such as simple numerical screening functions on the basis of molecular-level insight to help eliminate sequences of undesirable binding strength. The success of such higher-level approaches, however, yet depends on understanding the nature of the molecular interactions.