New insight into curcumin tethered lanthanum carbonate nanospheres and protein corona conferring fluorescence enhancement based sensitive detection of Amyloid-β aggregates

Abstract

The interfacial nano-bio complexion phenomenon provides the enhanced biological response via tagging of the biological moieties on the nanoparticle surface. The dynamic state of the protein-nanoparticle corona makes it suitable for protein quantification, targeting drug delivery and diagnostics applications. Herein, our approach molecular chemistry and optical characteristics of curcumin were used to elucidate the lanthanum carbonate nanospheres (REM100) and proteins interactions. The REM100 were prepared via novel, mix surfactant assisted homogeneous precipitation route. The spontaneous binding of Casein, Human Serum Albumin (HSA), Lysozyme (LZ) and Bovine Serum Albumin (BSA), Aβ monomer and Aβ aggregates on Curcumin-REM100 has been observed by protein concentration dependent steady-state fluorescence enhancement of the curcumin. Langmuir protein adsorption model elucidates the maximum surface coverage and an apparent dissociation constant parameter for Casein, Human Serum Albumin (HSA), Lysozyme (LZ) and Bovine Serum Albumin as interacting proteins. The curcumin form a stable hard corona layer over REM100 surface and accommodates the proteins as soft corona could be possible mechanism observed by steady-state fluorescence anisotropy. Based on all experimental outcomes we demonstrated, curcumin-REM100 as an efficient fluorescent probe performing compositional quantification of proteins in the nanoparticle-protein corona and able to delineate the monomer and the aggregate state of Amyloid-β with the Limit of detection of 0.2 ±0.045 μM, 30 times more sensitive then Thioflavin T (ThT). The protein-nanoparticle-based methodology optimized were showed great promising feature with its potential to develop as quick and sensitive detection of altered proteins.