Mutations of tumor suppressor protein p53 are present in almost about 50% of all cancers.
It has been reported that the p53 mutations cause aggregation and subsequent loss of p53 function,
leading to cancer progression. Here in this study we focus on the inhibitory effects of cationic osmolyte
molecules acetylcholine chloride, and choline on an aggregation prone 10 amino acid p53 mutant
peptide WRPILTIITL, and the corresponding wildtype peptide RRPILTIITL in vitro. The characterization
tools used for this study include Thioflavin- T (ThT) induced fluorescence, transmission
electron microscopy (TEM), congo red binding, turbidity, dynamic light scattering (DLS), and cell
viability assays. The results show that acetylcholine chloride in micromolar concentrations significantly
inhibit p53 mutant peptide aggregation in vitro, and could be promising candidate for p53
mutant/ misfolded protein aggregation inhibition.
Keywords: Aggregation, acetylcholine chloride, p53 peptide, osmolytes, cancer, inhibition.
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