Delineating the effect of trehalose nanoparticles on aggregation pattern of apo-α-lactalbumin protein: A nano-approach towards counteracting proteinopathies

Investigation of protein aggregation is a challenging and daunting task as it is associated with many amyloid-related diseases like Alzheimer's, Parkinson's diseases, etc. Sugar-based osmolytes are known to stabilize proteins under stress, however, their role in inhibiting protein aggregation is ambiguous. The role of molecular trehalose on the aggregation pattern of apo-alpha-lactalbumin protein (apo-α-LA) was studied earlier in our lab. In this study, we have utilized trehalose nanoparticles (TNPs) as an anti-aggregation agent against the thermally aggregated apo-α-LA. The effect of TNPs on the aggregation profile of apo-α-LA was observed by multi-spectroscopic and microscopic approaches, wherein UV–Vis spectroscopy, ThT assay, ANS fluorescence as well as Rayleigh scattering demonstrated that TNPs effectively prevent apo-α-LA aggregation when compared with molecular trehalose. Further validation was carried out with confocal microscopy that also supported the role of TNPs in preventing aggregation of apo-α-LA. Here, the effect of TNPs on the aggregation pattern of apo-α-LA was found to be a better than molecular trehalose, which advocates the application of nanotechnology to counter neurodegeneration. We believe that the inferences drawn from this study may suggest that the nanoparticle form of biocompatible sugar-related osmolytes can act as anti-aggregation agents toward protein aggregation.