Inhibition of Human Serum Albumin Fibrillation by Two-Dimensional Nanoparticles

Abstract

The formation and deposition of amyloid fibrils have been linked to the pathogenesis of numerous debilitating neurodegenerative disorders. Serum albumins serve as good model proteins for understanding the molecular mechanisms of protein aggregation and fibril formation. Graphene-based nanotherapeutics appear to be promising candidates for designing inhibitors of protein fibrillation. The inhibitory effect of graphene oxide (GO) nanoparticles on the fibrillation of human serum albumin (HSA) in an in vitro mixed solvent system has been investigated. The methods used include ThT fluorescence, ANS binding, Trp fluorescence, circular dichroism, fluorescence microscopy, field-emission scanning electron microscopy, and high-resolution transmission electron microscopy. It was observed that GO inhibits HSA fibrillation and forms agglomerates with β-sheet rich prefibrillar species. Binding of GO prevents the formation of mature fibrils with characteristic cross-β sheet but does not promote refolding to the native state.

Human Serum Albumin in the Presence of AGuIX Nanoagents: Structure Stabilisation without Direct Interaction

“…Literature shows that NPs have both inhibitory and stimulatory activity in the process of protein fibrillation [49][50][51]. It was observed by Bag et al [52] that graphene-based nanotherapeutics prevent the formation of HSA fibrils. However, cerium oxide NPs were found to promote protein fibrillation, as reported by Sekar et al [53].…”

Polyphenol capping on a gold nanosurface modulates human serum albumin fibrillation

“…Images of HSA solutions when incubated alone at 65 1C displayed entangled networks of long fibrils, and these observations are found to be similar to those of earlier works. 26,52,53 Co-incubation of SAuNPs resulted in protein absorption on the nanoparticle surface and the generation of a disorganised network of protein aggregates. A further reduction of fibrillar networks and the presence of amorphous protein aggregates on gold nanosurfaces were observed in the case of QAuNP and GAuNP co-incubated HSA samples.…”

“…23 Though 37 different proteins have been reported to cause amyloid diseases, 24 human serum albumin (HSA) is extensively used as one typical a-helical (460%) protein to understand the mechanisms of the misfolding and fibrillation process. 25,26 HSA is a physiologically prolific, single chain protein containing 585 amino acids arranged in three homologous domains. 27 The literature has shown that the systematic aggregation of albumin occurs through partial misfolding of its native structure and the process has been conveniently replicated in vitro through specific conditions such as high temperature, metal ions, treatment with denaturing chemicals, and lowering of pH.…”

Destabilization of amyloid fibrils on interaction with MoS2-based nanomaterials

“…36 In addition, many investigations have shown that carbon based nanomaterials such as fullerenes, carbon nanotubes, graphene and graphene oxide could be useful to inhibit the aggregation of amyloid peptides and to destroy matured brils. [37][38][39][40] The hydrophobic interaction of fullerenes gives a size-dependent destabilization of the bril structure. 41,42 It has been shown that carbon nanotubes inhibit the formation of aggregates from amyloid beta peptides (16)(17)(18)(19)(20)(21)(22).…”