Abstract

Mutation in genes which encode amino acids as well as any other adverse condition can lead to neurodegenerative diseases like Alzheimer's, diabetes mellitus, Huntington’s etc. Transition from α helix to β sheet is the main hallmark of the formation of aggregates which may lead to fibril or amyloid formation. Human Serums Albumin (HSA) being major carrier protein was taken as model protein to investigate the effect of Melamine (an organic compound). Melamine (MM) toxicity has recently attracted worldwide attention as it causes renal failure and the death of humans and animals. In vitro analysis through various spectroscopic methods has revealed that melamine can cause the unfolding of HSA under certain conditions. Increment of fluorescence intensity and disappearance of two negative peaks in circular dichroism spectroscopy have indicated that β sheeted structure is favoured with gradual increase in concentration of melamine upto 225 μM. It was further confirmed by Transmission electron microscopy. Interactions between protein and ligand were also analysed by autodock. Finally, fluorescence microscopy has corroborated the presence of aggregates in our sample of interest.

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