Microscopic Mechanism of Specific Peptide Adhesion to Semiconductor Substrates

TL;DR

This study combines experimental and computational methods to uncover how specific peptide sequences, especially mutations, influence adhesion to semiconductor surfaces, advancing understanding of peptide-surface interactions for nanotech applications.

Contribution

It introduces a hybrid peptide-substrate model and demonstrates how sequence mutations affect peptide adhesion to silicon, validated by experiments.

Findings

Proline mutation enhances binding affinity to silicon.

Sequence-dependent adhesion specificity observed.

Validated computational predictions with atomic force microscopy.

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.