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Study of structural and dynamic properties of alpha-synuclein
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Neurological diseases are gaining an important role in the death rate in the developed world. Besides that, the current treatments for these types of diseases only serve as a symptomatic relief, and do not serve as an actual solution for the issue. Parkinson’s Disease fits the aforementioned profile, and it is known for degrading the quality of life of the affected individuals, causing dementia, slowness of movement, and eventually death.
Many of these diseases are caused by pathological agents known as prion-like proteins, one of them being alpha synuclein, which is the one currently attributed as being responsible for Parkinson’s.
This study focuses on the dynamic and structural changes which occur to alpha-synuclein when exposed to different external factors. Moreover, this study also aims to compare the data gathered from these tests and compare it with tests already made on prion exposed to the same conditions.
With that aim, the studies were first directed to varying the protein concentrations between 0,05 M and 80 M (the same concentration range studied on prion), altering the pH of the medium, the type of buffer utilized, and also the effect of oxidative stress. The effects caused by these changes were then studied by utilizing mass spectrometry, ion mobility spectrometry, size exclusion chromatography, MALDI, and peptide analysis after a trypsin digestion.
With this study it was confirmed the existence of modifications in the conformations of alpha-synuclein by changing its concentration and the pH of the medium. It was also possible to notice some changes in its behavior due to oxidative stress which are similar to the ones seen in prion but unlike prion which creates large oligomers, alpha synuclein only creates dimer.
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Alpha-synuclein Prion-like Mass spectrometry Parkinson’s