Blood Magnet

Did I get your attention? Great. It's not clickbait.
I have been looking at this paper for a couple days now, and we've got a legit lab, so here we go people. Tear it down, tell me how this isn't a thing. Otherwise, we're gonna start working on this in the next week.

http://sci-hub.tw/10.1038/nmat4484

tldr; eli5
magnetic receptor structure co compound that works with a buddy system that has been shown to show spontaneous alignment in magnetic fields. In your bloods. May form the basis of magneto reception in other animals.

So, how does this get weird, what are the roadblocks?

Comments

  • Are you proposing designing a MagR compatible with human blood?

  • MagR-Cry complex expressed is the key point here.

  • It's an interesting study.

    However, "Therefore, a magnetosensitive nanoscale biocompass would be assembled by
    the combination of photoreceptors (Cry) and magnetoreceptors (MagR), a complex that we define as the magnetosensor.....This putative magnetoreceptor protein (MagR) forms a rod-like complex with Cry, and co-localizes with Cry in the pigeon retina."

    I don't see how you could easily get the complex to express in blood within the body.

    To induce the development of the complex in a human retina would require successful modification of the neural precursor cells that develop into the retina. From what I have read they're one of the most difficult types of progenitor cells to access, and I couldn't find anything on how often our retinal cells are replaced, if they ever are.

    My suggestion would be to try to induce the development of this complex in lab rats and go from there.

    Your secondary challenge would be to determine if the resultant data from the modified photoreceptors is even something the human brain can process in any meaningful way.

  • edited January 2018
    Hmm good point there. I'll probably go with some cells in vitro testing pre murine testing, but yeah
  • I think the photoreceptor aspect of this might be really important. I wonder if the reason this requires light exposure to work is because normally things aren't magnetic at such a small size. that whole protein has maybe 10 FeS clusters tops which is an absurdly small amount of magnetic material. Normally you need much much more material to maintain magnetism. I suspect that the exposure to light induces a bit of charge movement in the complex which helps to align the spins of the feS clusters and potentially pull off some electrons to allow it to be intrinsically magnetic.

    I need to read more to see how it hands off any signal it generates to the retinal cells to be interpreted as information. Cause that's probably the most important part

    Only 1 version of cry and MagR actually come together to form the complex. For birds that's dcry4 and then MagR. So you'd need to provide the dcry4 since humans don't produce it, but we should have the MagR gene already. I'll need to double check to confirm that.

    I think the ideal way to test this under perfect circumstance would be in some neuron cell lines and ideally a retinal cell line. In magical wonderful land, you'd want to grow these in one of the petri dishes with the tiny wire traces printed on the surface of the dish so you can connect up some electrode and see if the neurons fire when you pass a magnet over it. I worry that you'd have signal contamination though because the moving magnet would induce currents in the small wires potentially so I dunno.

    The simplest test would be to just do this in hek cells and then stick a magnet next to the flask and see if the cells move. That'd be a great indication that this works. Cause if they do, then you could just make this into a plasmid with a neuron specfic promoter and then apply it locally with DMSO/lipofectamine to the area you want to be magnetic. If the proteins form in parcinian corpuscules or similair, the motion should cause them to fire. All of this assuming of course that light isn't needed to make the thing magnetic. So the HEK cell test would allow us to figure lots of things out at once; how important is the light exposure, is the protein inherently magnetic, is it strong enough to yank cells around, will producing these proteins harm cells.

  • cool, let's do it.
    anyone else got any input?

  • did some more reading, found this https://www.ncbi.nlm.nih.gov/pmc/articles/PMC521149/

    different paper that talks about the interaction between cryptochrome proteins, neurons, and this other protein called c-fos that's also expressed in the same areas. f-cos is part of AP-1 which controls gene expression amongst other things. I'm trying to find evidence for it triggering neurons to fire. In the paper they talk about the importance of light for at least the bird version of the protein complex. More importantly they mention that the magnetosensing only works during the day, specifically when the bird is exposed to blue or green light. Doesn't require a lot of light, but needs some. In the original paper they talk about the mechanism of how the protein complex is magnetic. They mention that it is ferrimagnetic, so I suspect that absorbing the light is "suppressing" one set of electron spins in the FeS clusters. This way they have an innate magnetic field and can point in the direction of an applied field by their magnetic field aligning.

    I was looking at some of the immunofluorescent images and it sort of looked like the MagR proteins were near the membrane of the neurons. I dunno, could just be seeing things, but if true could point to an interaction between a structural element or gated channel such that it's motion could trigger neurons firing.

    So ya, we should get some retinal cells and some other neuron cell type, make them express these proteins and then do some testing. See how they both respond, with and without light. Should also look into different varieties of the protein from species that work in the dark

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