The biological significance of protein aggregating diseases of the nervous system has considerably increased during the last decade. While knowing the human neurodegenerative disorders such as Alzheimer\'s disease (AD), Parkinson\'s disease (PD), Amyotrophic Lateral Sclerosis (ALS), Creutzfeldt Jakob Disease (CJD) for a long time, a large body of researches are getting focused on Bovine Spongiform Encephalitis (BSE), as its biological-economical importance, as well as the wild and uncontrollable nature of this prion caused neurodegenerative disorder is widely threatening the human society. However, our knowledge about BSE is much less than it should be, as the high infectivity properties of proteinase resistant species of prion protein (PrP-res) makes this peptide more complicated to be used directly in biological studies. Herein, we introduced a specific sequence of the peptide amyloid-beta (1-42) which shows high aggregating behavior, as well as neurotoxic properties in cultured rat primary neurons isolated from 17d old rat fetus neuronal stem cells. Using the In-cell western analysis the neurotoxicity of this aggregated form of the peptide was shown as a decrease in cell-structural beta-tubulin protein immunoreactivity. We have also evaluated the genotoxic properties of this peptide sequence using COMET assay by measuring the area of the genomic DNA shift by fluorescent microscope imaging under a field of electrical charge. These aggregating neurotoxic/genotoxic properties of amyloid-beta if to be hold true in vivo as well, makes it of benefit to be used as a bio-safe alternative for PrP-res in biological studies.

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