Microscopic Mechanism of Specific Peptide Adhesion to Semiconductor Substrates

Details Microscopic Mechanism of Specific Peptide Adhesion to Semiconductor Substrates Microscopic Mechanism of Specific Peptide Adhesion to Semiconductor Substrates

2011-07-06

arxiv.org/abs/1107.1208v1

Angew. Chem. Int. Ed. 49, 9530-9533 (2010); German Edition: Angew. Chem. 122, 9721-9724 (2010)

Physics

Condensed Matter

Mesoscale and Nanoscale Physics

14 pages, 4 figures

Scientific paper

The design of hybrid peptide-solid interfaces for nanotechnological applications such as biomolecular nanoarrays requires a deep understanding of the basic mechanisms of peptide binding and assembly at solid substrates. Here we show by means of experimental and computational analyses that the adsorption properties of mutated synthetic peptides at semiconductors exhibit a clear sequence-dependent adhesion specificity. Our simulations of a novel hybrid peptide-substrate model reveal the correspondence between proline mutation and binding affinity to a clean silicon substrate. After synthesizing theoretically suggested amino-acid sequences with different binding behavior, we confirm the relevance of the selective mutations upon adhesion in our subsequent atomic force microscopy experiments.

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