HI all,
I would like to know if there are any papers regarding beta-synuclein aggregation in vitro. I have seen papers where they show low percentage of SDS can induce beta-synuclein but does it aggregate by itself?
http://www.ncbi.nlm.nih.gov/pubmed/?term=beta+synuclein+AND+aggregation
beta syn is considered as the non-amyloidogenic analogue of alpha syn, there are also some papers showing that the N-termini fragment (1-15) of beta-syn is able to stop the aggregation of alpha in vitro. It do not contains the NAC region. There are not evidence in vitro, from my knowledge, that beta is able to aggregate.
Found the right buffer conditions, most proteins would aggregate and many adopt well ordered fibrillar structures, since this state is, perhaps, the most stable folded state of a protein. In the particular case of synucleins, alpha-synuclein has a strong tendency to form these structures in vivo and cause disease, a property only shared by a few proteins. Beta-synuclein has a lower tendency than alpha-synuclein to form these structures in vivo, and only does so in vitro under particular buffer conditions such as the presence of lipids, detergents and metal cations. There are quite a number of biophysical studies that addressed this feature of beta-synuclein in a comparative manner with alpha-synuclein, most of them from the Dobson group in Cambridge, UK
my co-worker do the experiment for beta synuclein aggreagating assay
and consistent with some research show that beta-synuclein do not aggregate since that beta synuclein do not have NACregion for formating the nucleic , his data shows that beta synuclein is hard to aggreagate from CD assay and Thio-T assay
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