Résumé
The possibility to engineer bio-nanomaterials with programmed synthesis and controlled immobilization of biomolecules through biomimetic molecular evolution approach has been demonstrated. Material specific peptides with exquisite molecular recognition function were used as a linker for the attachment of biomolecules. Exploring the origin of peptide material specificity not only opens up rational design approach with precise control over biomimetic bio-sensor design, but more importantly provides a new route of functionalizing for various material surfaces with enhanced sensitivity over classical grafting chemistry. To study the fine prints of experimentally obtained peptides, theoretical understanding of surface interactions may serve as important clues for further refinement. By taking advantage of classical molecular dynamics (MD) simulations and density functional theory (DFT), we investigated the origin of this smart recognition function through the strength of interaction of experimentally selected 12mer peptides revealing high binding affinity towards n+-Si(100). Here, we attempt for the very first time to model the interaction of the peptides (in buffer solution) with semiconductors and we calculate their binding energies at the atomic level, enabling thereby linking direct evidence to our experimental evidence. Several peptide conformations have been taken into account simultaneously upon the surface. Our studies demonstrate that the peptides possess certain recognition function and their high interaction energy with the surface makes them unique among the populations. Our work is a step towards the understanding of the interactions between peptides and semiconductor surfaces that is a highly relevant challenge in the development of novel devices with a high degree of biocompatibility as well.