Disorder in the Brain: Proteins Gone Bad
Protein misfolding and aggregation is a hallmark of incurable neurodegenerative diseases like Alzheimer’s (AD), Parkinson’s (PD), and some dementia types. Immense efforts are underway to clarify the underlying mechanisms responsible, of which the consequences phosphorylation contributes remain incompletely understood. For example, the causative versus the consequential role of site-specific phosphorylation of aggregate-forming alpha-synuclein (aSyn) in PD continues to be contested.1,2 Moreover, hyperphosphorylation of the tau protein in AD and some types of dementia is known to drive its misfolding and aggregation, but the pathophysiological ramifications also continue to be challenged.2,3
Therefore, in addition to physiologically-relevant in vivo models, accurate technical approaches are vital for the proper study of protein behavior, since this research primarily drives the development of novel biomarkers and therapeutics. To that end, mass spectrometry (MS) is utilized to precisely determine both the extent and location of phosphorylation present on protein(s)-of-interest, which together inspires their biological functions.
Breaking Down Complex Neurodegenerative Disease with Mass Spectrometry
Researchers have two source options for MS analysis of in vivo samples: the cerebrospinal fluid (CSF) or post-mortem diseased brain ...
