Friday, February 3, 2017

Super deep proteomics on 17 brain regions in mice with Parkinson's!

Okay...this is kinda great!

Neuroproteomics is hard -- the brain is a complex thing. Material is limited -- there are tons of lipids -- protein profiles change markedly as you move spatially throughout the brain.

But Parkinson's totally sucks. And it looks like it is definitely a protein mediated disease so we need to be involved in working with -- and eventually eliminating this turd of a disease.

In this brand new study from Sung Yun Jung et al., they show a really impressive way of working around these challenges!

Using a mouse model for Parkinson's they excise a 1mm squred region in the central area of 17 (!!) different anatomical brain regions. As you might guess...this isn't an awful lot of material. They employ a really interesting 2D separation methodology and use an Orbitrap Fusion to get a really impressive sequence coverage depth.

They go after a global quan approach -- but go back in with parallel reaction monitoring for validaton and to better improve their sensitivity.  Interestingly, it looks like they used high resolution MS1 for quantification (120,000 resolution) and used the ion trap fragmentation for confirmation. A bit of a different twist on the reminds me of a more targeted application of the WiSIMDIA technique -- and I bet Skyline doesn't care, it'll just process the data expertly!

The results...? One of the best models of the proteomic content of mouse brain organelles ever -- and definitely the best coverage of the same for a mouse Parkinson's model!!

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