The mechanism of amyloid fibrillation persists as one of the more difficult problems within the realm of biochemistry and is associated with several pathological conditions. The etiological nature of this reaction has provoked numerous studies, though the thermodynamic stability of the fibrils combined with the neuro-specific mediums in which they form remain insurmountable obstacles. Therefore, compounds that could kinetically impede this reaction are of particular interest. In this work, we assessed the inhibitory potential of pegylated gold nanoparticles using human insulin as model protein. Insulin serves as a readily available analogue to many of the amyloid-forming proteins found in the brain, undergoing the same conformational change from a primarily α-helical structure to β-sheets. Combination of spectroscopic and microscopic techniques was used to elucidate the role of particle’s surface charge and chain length on the rate of fibrillation. Our preliminary findings show a potential link between the presence of pegylated gold nanoparticles and slower rates of insulin aggregation.

Role of PEGylated gold nanoparticles on insulin fibrillation

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