LAUSR

Significance Protein malfunction and misfolding have long been associated with the onset and development of neurodegenerative conditions such as Alzheimer’s and Parkinson’s diseases. Protein misfolding/aggregation proceeds via primary nucleation whereby proteins can convert from their normal physiological forms into pathological amyloid aggregates. The presence of interfaces plays an important role in this aggregation phenomenon and can dramatically modulate nucleation, either by accelerating or inhibiting aggregation. Through coarse-grained computer simulations, kinetic theory, and measurement of the Gibbs free energy of adsorption, we show that systems which have high affinity to adsorb to an interface display delayed kinetics, whereas systems that have low affinities have similar behavior, suggesting a maximum between the two regimes (nonmonotonic behavior) where the aggregation rates are highest.