Deep Literature Dive and Beginning of Lab Work

Hello everyone,


For my research project this summer I have taken a look at the cause of human neurodegenerative diseases through an evolutionary lens. The first part of these past 7 weeks was to undergo a deep dive into the primary literature surrounding Amyloid Beta. Amyloid beta is the prion that I am choosing to study because of its close connection to Alzheimer’s disease and has been the subject of intense research for the past 40 years.


As you can imagine from that extensive amount of time there is an enumerable number of papers published on the topic which made the review process quite difficult. There were two reasons for spending so much time in the thickets of dense scientific papers. The first reason for the review was that I wanted to have a complete handle on all aspects of knowledge surrounding Amyloid Beta and its sister prions. The second reason was to unearth the genetic sequences I would need to create a synthetic human Amyloid Beta prion that could also live and function in a yeast cell. A big hurdle I needed to overcome was I wanted to study a human prion in yeast cells, so I needed to create a chimeric protein, or synthetic protein made up parts of a bunch of different proteins like a cyborg of sorts. This chimeric protein need to allow for the human prion properties to remain, through the conservation of the important prion sections of the human Amyloid Beta, but also allow for it to thrive in a yeast cell through the conservation of all the other important parts of a yeast prion.


What my research unearthed was a yeast prion called SUP35 has been used in the past for this exact purpose because it provides a chimeric prion structure that can thrive in yeast. The unique part about this is that by substitute a small chunk of SUP35 called the prion domain with a the prion domain of the prion of interest, in this case Amyloid Beta, you can study the prion of interest in the highly manipulative environment of yeast. Once I understood this I set out to figure out the genetic sequences of the prion domains as well as the total sequence of the SUP35 prion protein. I then did the swaps and finally sent out the new synthetic sequence for creation. It was a very time intensive process with over 3,000 base pairs to type and keep track of. This process alongside writing a literature review of the important things I discovered when learning about Amyloid beta took up all of my time for the first few weeks of this summer.

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