Approximately 10% of neurodegenerative diseases can be attributed to genetic disorders, while the remaining 90% are sporadic, suggesting that environmental factors may play a role in the iniation. An environmental neurotoxin β-Methylamino-L-alanine (BMAA) has been identified to potentially play a role in the formation of sporadic neurodegenerative diseases. Detection of BMAA in diseased brains has led to a hypothesis of BMAA incorporation into proteins potentially resulting in protein aggregation. This study aimed to explore methodologies that could identify whether BMAA is present within the detectable proteome.
Several neuroblastoma SH-SY5Y cell cultures were treated with a range of BMAA concentrations. Unfractionated and fractionated digests of treated SH-SY5Y cells were analysed by both data dependent and independent LC-MS/MS. Bioinformatic analyses were performed utilising PEAKS studio X.
No incorporation of BMAA was detected with confidence in place of any amino acid. These results indicate that further research on the incorporation of BMAA into proteins is not feasible with traditional proteomic methodologies
Data collected in this study suggest that BMAA may not be incorporated into proteins by traditional protein synthesis but instead might be bound to proteins in another manner. Furthermore, this research indicates that if BMAA is incorporated into proteins, then detection of BMAA within proteins is not feasible with short term culture and simple proteomic methodologies.