Microscopic Mechanism of Specific Peptide Adhesion to Semiconductor Substrates
Abstract
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.
- Publication:
-
arXiv e-prints
- Pub Date:
- July 2011
- DOI:
- 10.48550/arXiv.1107.1208
- arXiv:
- arXiv:1107.1208
- Bibcode:
- 2011arXiv1107.1208B
- Keywords:
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- Condensed Matter - Mesoscale and Nanoscale Physics;
- Condensed Matter - Soft Condensed Matter;
- Condensed Matter - Statistical Mechanics;
- Quantitative Biology - Biomolecules
- E-Print:
- 14 pages, 4 figures