LAUSR

The accumulation of protein aggregates (tau) causes Alzheimer's disease (AD), Parkinson's disease (PD), and a range of neurodegenerative diseases. To develop a less toxic and bio-derived nanomaterials for inhibition of protein-aggregation, carbon nanodot has been used for this study. Nanodot have generated huge interest in biomedical applications owing to unique emission property and good biocompatibility. A carbon nanodot is synthesized from a natural resource-lemon juice and glutathione. The synthesized nanodot possesses excitation-independent emission and nano-sheet like with high graphitic content. Interaction of protein with CND is monitored by intrinsic fluorescence (trp residues), FT-IR and circular dichroism spectroscopy. Whereas it solubilizes the protein aggregates at its higher concentration. Both induced-aggregation and co-solubilization are sequence-independent and dictated by nanodot. The study may shed light on the role of glutathione in glutathione-dependent glyoxalase system toward defence against glycation product.