Self-assembly of plant protein fibrils interacting with superparamagnetic iron oxide nanoparticles

In situ fibrillation of plant proteins in presence of the superparamagnetic iron oxide nanoparticles (NP) promoted formation of a hybrid nanocomposite. The morphology of NP-fibril composite was revealed using ex-situ atomic force microscopy (AFM) in air. The NP-fibrils were associated into extended multi-fibril structures, indicating that the addition of NPs promoted protein association via beta-sheet assembly. Real-time movement of NPs attached to fibrils under an external magnetic field was visualized using in-situ AFM in liquid, revealing that composite structures were stable at low pH, and displaying dipolar property of the NPs in the composite at high pH. Changes in magnetic properties of NPs when interacting with protein fibrils were quantitatively mapped using magnetic force microscopy (MFM). The magnetic moment of the NPs in composite was increased by co-existing with protein at low pH, while their dipolar nature was maintained at high pH. Self-assembly of the protein into fibrils is accelerated with increasing NP concentration within an optimal range, which is attributed to a fibrillation-competent conformation of the peptides. The latter was explained by the formation of favorable hydrogen bonds, electrostatic interactions, and efficient surface energy transfer between NPs and proteins.