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The design of hybrid peptide-solid interfaces for nanotechnologicalapplications such as biomolecular nanoarrays requires a deep understanding ofthe basic mechanisms of peptide binding and assembly at solid substrates. Herewe show by means of experimental and computational analyses that the adsorptionproperties of mutated synthetic peptides at semiconductors exhibit a clearsequence-dependent adhesion specificity. Our simulations of a novel hybridpeptide-substrate model reveal the correspondence between proline mutation andbinding affinity to a clean silicon substrate. After synthesizing theoreticallysuggested amino-acid sequences with different binding behavior, we confirm therelevance of the selective mutations upon adhesion in our subsequent atomicforce microscopy experiments.

Microscopic Mechanism of Specific Peptide Adhesion to Semiconductor Substrates