Protein aggregation
leads to the transformation of proteins from
their soluble form to the insoluble amyloid fibrils and these aggregates
get deposited in the specific body tissues, accounting for various
diseases. To prevent such an aggregation, organic–inorganic
hybrid nanocomposites of iron oxide nanoparticle (NP, ∼6.5–7.0
nm)-conjugated cellulose nanocrystals (CNCs) isolated from Syzygium cumini (SC) and Pinus roxburghii (PR) were chemically synthesized. Transmission electron microscopy
(TEM) images of the nanocomposites suggested that the in situ-synthesized
iron oxide NPs were bound to the CNC surface in a uniform and regular
fashion. The ThT fluorescence assay together with 8-anilino-1-naphthalenesulfonic
acid, Congo Red, and CD studies suggested that short fiber-based SC
nanocomposites showed better inhibition as well as dissociation of
human serum albumin aggregates. The TEM and fluorescence microscopy
studies supported similar observations. Native polyacrylamide gel
electrophoresis results documented dissociation of higher protein
aggregates in the presence of the developed nanocomposite. Interestingly,
the dissociated proteins retained their biological function by maintaining
a high amount of α-helix content. The in vitro studies with
HEK-293 cells suggested that the developed nanocomposite reduces aggregation-induced
cytotoxicity by intracellular reactive oxygen species scavenging and
maintaining the Ca2+ ion-channel. These results indicated
that the hybrid organic–inorganic nanocomposite, with simultaneous
sites for hydrophobic and hydrophilic interactions, tends to provide
a larger surface area for nanocomposite–protein interactions,
which ultimately disfavors the nucleation step for fibrillation for
protein aggregates.