▎ 摘　　要

Protein and peptide aggregation/fibrillation is reported to be responsible for several neurological disorders. Fibrillation of the amyloid beta-peptide fragment (25-35) which is a biologically active region of the full length peptide, has been observed to be significantly inhibited in presence of the two dimensional nanomaterial graphene oxide (GO). Fibrillation and inhibition of the A beta(25-35) peptide by GO has been performed at 37 degrees C at physiological pH (pH 7.4). The inhibition process is monitored by Thioflavin T fluorescence (ThT), circular dichroism spectroscopy, matrix assisted laser desorption/ionization mass spectrometry, dynamic light scattering experiments etc. The soluble fraction of the protein is quantified by the BCA assay. Microscopic techniques are used to study the morphology of the fibrils formed. GO is observed to inhibit the fibrillation even at very low concentrations and is amplified with increase in concentration of GO. ThT kinetic data fitted well with a sigmoidal curve and shows that GO is able to lengthen the lag phase of the fibrillation process. It appears that surface adsorption of protein on the nanomaterial prevents the monomers to come together. It is speculated that the presence of both polar and non-polar moieties in GO interact strongly with the hydrophobic and hydrophilic residues of the A beta(25-35) peptide monomer units, thus preventing further aggregation.