Huntington’s disease, Parkinson’s disease, Alzheimer’s disease, Prions Disease are few among many diseases caused due to the aggregation of misfolded proteins, which eventually leads to the formation of amyloids. Amyloids contain a large amount of â – sheets which make it highly stable in the body environment, thus making its lysis difficult. It is reported that the misfolded proteins form amorphous aggregates first which contain less number of â – sheets. These aggregates would further form amyloids as the number â – sheets increase. Inhibiting the formation of aggregates can be regarded as a therapeutic approach in the treatment of above mentioned diseases. In the present investigation, two existing protocols for the formation of amorphous aggregates of lysozyme (Lys) were studied and a novel protocol for the same was proposed. This novel protocol showed high amounts of aggregate formation of lysozyme under laboratory conditions, as observed under Thioflavin T (ThT) assay. However, there was no formation of amyloids, as was observed under Congo Red assay. The effect of DMSO and Glycerol was investigated on the formation of Lysozyme aggregate. The results of these assays indicated that there was significant decrease in the amount of aggregation of lysozyme in solution. Thus, it was concluded that DMSO and Glycerol act as inhibitors for lysozyme aggregation
