Alzheimer’s? Forget about it!
Let’s face it, diseases that affect the brain are some of the hardest to deal with. Anyone who’s lost someone to alzheimer’s knows exactly what I am talking about. Looking at someone you love and watching them slip away without any visible difference can be heart wrenching!
However, there is a new hope! Physicists [of all things] from Michigan State University published an article in the Journal of Biological Chemistry, that might make alzheimers and associated diseases a thing of the past.
First, what causes things like alzheimers? Well it turns out [the most likely candidate] for the onset for these diseases are prions. That name might sound familiar if you have read anything about mad cow disease. Prions are misfolded proteins that get built up in the brain and in the case of cows, causes [you guessed it] mad cow disease.
[Loony Hint: A protein is just a long chain of amino acids, just think of a protein as a piece of paper, the amino acids would be words on that paper. The body folds that protein like origami, and just like origami if it is folded wrong it will not do anything it was supposed to do. And that duck might end up looking like a folded piece of paper, don’t worry happens to me too.]
Well the team found a “molecular tweezer” that keeps the proteins from clumping or aggregating [bunching together, or bumping] when they are being folded. Lisa Lapidus, MSU associate professor of physics and astronomy [the co-author of the paper] correlated the speed at which an unfolded protein changes shape, or reconfigures, with its tendency to clump or bind with other proteins.
They found that if the folding [ also called reconfiguration] happens faster or slower than the proteins bump into each other, aggregation [or build up] is slow. However, if they bump about as quickly as they fold, well then aggregation is high.
[Loony hint: High aggregation = bad news bears, yes it’s a technical term]
All this means the researchers needed to find something to keep folding speed high and bumping low. Lapidus’ original research involving the spice curcumin, which proved promising, but could not get past the blood brain barrier [the thing keeping bad stuff in the blood away from the brain!!]. So while it was a good starting point, it was not going to be what they needed.
Luckily they found something another candidate for the job, the molecule, CLR01, which was patented jointly by researchers at the University of Duisburg-Essen (in Germany) and UCLA does the trick. CLR01 binds to the protein and speeds up folding, thus keeping aggregation low. It is sort of like a little molecular claw that attaches to a specific amino acid on the protein [lysine for those interested] and speeds up the reconfiguration [folding] process.
The CLR01 molecules cross the blood brain barrier AND speed up reconfiguration even better than curcumin did, a definite plus. Not only that, but CLR01 went exactly where it was needed. The results from the study are more than just promising, so much so that one of the co-authors is using a fairly new tool, crowdsourcing, to raise funds for the clinical trials. You can donate or find out more — here!!!
This means [with luck] we will be seeing those clinical trials [as in on humans] very soon. Who knows, soon we may be telling scary stories about big bad alzheimers and the other brain diseases instead of having to live with it.
All this is very exciting so again, please if you can, donate to this research! One more time the link is indiegogo.com [that goes to the specific page.]
Wishing you could forget all the metaphors I used? Well then you probably want the more technical stuff, like the full study, which can be found — here!
Acharya S., Safaie B.M., Wongkongkathep P., Ivanova M.I., Attar A., Klarner F.G., Schrader T., Loo J.A., Bitan G. & Lapidus L.J. & (2014). Molecular Basis for Preventing α-synuclein Aggregation by a Molecular Tweezer, Journal of Biological Chemistry, 289 (15) 10727-10737. DOI: 10.1074/jbc.M113.524520