Effect of surface structure on the adsorption and conformation of an amyloidogenic peptide

Surfaces, both synthetic and natural, have long been known to influence the aggregation of proteins into supramolecular structures, including amyloid fibrils. Whether a surface promotes or inhibits fibril formation depends on its physiochemical properties, such as its surface chemistry and structure. While a number of studies have examined the effect of surface chemistry on this, the role of surface structure has been less well studied. Using molecular dynamics simulations the behaviour of a model amyloidogenic peptide, consisting of a short segment of amyloid-beta on surfaces consisting of alternating hydrophobic and polar stripes of varying width. The adsorption and conformation of the peptide depends on the stripe width, with stronger adsorption being seen on surfaces with larger hydrophobic regions. For the wider stripes, the conformation of the peptide is similar to that on the uniform hydrophobic surface, with these conformations being less fibril-like. This demonstrates the potential to use surface structure to control the conformation of peptides, with a subsequent influence on their aggregation and assembly.