Abstract

Understanding protein adsorption onto material surfaces is a major challenge in the design of biomaterials. While this has been long studied, knowledge of how the nanoscale surface structure affects protein adsorption is still lacking. Using molecular dynamics simulations the effect of nanoscale structure, specifically alternating hydrophobic and hydrophilic stripes, on the adsorption of LK-peptides onto surfaces is investigated. Strongest adsorption is found for surfaces with larger hydrophobic regions, which allow the peptides to minimise unfavourable contacts with hydrophilic regions. This information may be used to understand the relationship between protein adsorption and surface structure, allowing for control over biocompatibility and anti-fouling behaviour.

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