Nanoparticles Mediated Interventions in hIAPP Fibrillation: Implications for Aggregation Pathways and Toxicity

Over the past decade, the protein–nanoparticles (NPs) interaction studies have demonstrated strong affinity of proteins towards the NPs surface, resulting in the modulation of aggregation and fibrillation. The ability of NPs to intervene with the nucleation and fibrillation pathway of amyloid‐forming proteins and peptides depends upon their ability to modify the protein's conformational restructuring step and extent of which is governed by the type and strength of interactions involved therein. Various nonspecific interactions involved at the protein–NPs interface impart complexity to their interaction interplay, which in turn, may accelerate, retard, inhibit, or have no effect on fibrillation of proteins. In this review, we have summarized various types of NPs used to modulate the hIAPP fibrillation process associated with type II diabetes, highlighting the role of specific properties of NPs influencing their interactions with hIAPP and, in turn, the fibrillation. This understanding provides valuable insights into NPs‐mediated conformational changes in peptides affecting the nucleation, fibrillation, and related cytotoxicity.