Computer simulations of peptide folding, aggregation, and adsorption to solid substrates

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In recent experiments it could be shown that the binding of peptides to certain solid substrates is highly specific. It strongly depends on the amino acid sequence of the peptides and the properties of the adsorbing material. The principal mechanisms of the adsorption process are still widely unknown. It is not yet clear, whether this process is accompanied by a refolding of the peptide or whether it is a simple docking process without noticeable structural changes of the peptide. It is also not known how peptide aggregation in dense solutions influences the adsorption strength. The growing interest in understanding such organic-inorganic hybrid systems is explained by possible future biotechnological applications of nanosensory and nanoelectronic devices. In this project we first plan to perform Monte Carlo computer simulations in order to reveal the single-peptide folding properties of the synthetic sequences used in the experiments. In the next step aggregation in multiple-peptide systems at first without substrate shall be investigated. For these studies the all-atom model with reduced force field, developed by the Lund group, shall be employed. Eventually, this model is extended by incorporating the interaction with solid substrates and shall be exploited for hybrid peptide-silicon systems, for which experimental data are available.