Please Support Our Infrared Vision Project!
Hello grinders! @Cassox, @glims, @zombiegristle and I have been working on a project that we'd like to share with the community. We have developed a protocol that we believe may extend human sight into the near infrared range--all by means of a dietary shift!
As you know, what we call 'color' is actually the visual cortex' translated perception of different wavelengths of light; blue light is on the short end of the visual spectrum (eg ~400nm) and red light is on the long end (eg ~650nm). Light passes through the pupil and lens of the human eye and strikes the retina. On the retina are photoreceptive cells (rods and cones) which contain [i]photopigments[/i]. The photopigments in the human eye -- photopsin in the cones and rhodopsin in the rods -- are formed by the protein opsin and Vitamin A in the form of retinal. These photopigments are bipolar cells which are excited by a given range of light wavelengths--usually ~400-690Nm in humans--and in turn excite the visual cortex.
Many cold blooded animals, however, utilize [i]porphyropsin[/i] as their visual pigment. Porphyropsin is excited by a similar range of wavelengths as the human photopsin and rhodopsin, but is also excited by a far greater range of red light, even extending into the NIR in some species of freshwater fish. Porphyropsin is formed by opsin and 3,4-dehydroretinol, also called vitamin A2. In essence, we intend to completely cut vitamin A out of our diet and replace it with A2.
In order to provide valid scientific data for the community, we are adhering to a strict dietary regimen provided by the generous Mr. Rhinehart, the inventor of Soylent (www.soylent.me) and collecting data on visual spectrum shift changes via ERG. In order to purchase this equipment, we decided to crowdfund using the Microryza scientific research platform. We would greatly appreciate any financial assistance the community could offer this project--every dollar counts!!
All our results will of course be published free and open source following standardized research paper format, both on Microryza and on the publish.biohack.me page here. Our long-term goal, should this proof-of-concept experiment go well, is to develop a more permanent hack which inhibits vitamin A uptake and upregulates A2 uptake. The results of this later research will also be free and open source.
Here is our project page:
https://www.microryza.com/projects/can-we-biologically-extend-the-range-of-human-vision-into-the-near-infrared
Please feel free to ask any questions about the project or any suggestions to add to the project page here. Grind on!
Project members:
@glims --A2 production/sourcing; biochem
@Cassox -test subject; medical supervision
@Saal -test subject; shameless promotion; dead weight :P
@zombiegristle -test subject
As you know, what we call 'color' is actually the visual cortex' translated perception of different wavelengths of light; blue light is on the short end of the visual spectrum (eg ~400nm) and red light is on the long end (eg ~650nm). Light passes through the pupil and lens of the human eye and strikes the retina. On the retina are photoreceptive cells (rods and cones) which contain [i]photopigments[/i]. The photopigments in the human eye -- photopsin in the cones and rhodopsin in the rods -- are formed by the protein opsin and Vitamin A in the form of retinal. These photopigments are bipolar cells which are excited by a given range of light wavelengths--usually ~400-690Nm in humans--and in turn excite the visual cortex.
Many cold blooded animals, however, utilize [i]porphyropsin[/i] as their visual pigment. Porphyropsin is excited by a similar range of wavelengths as the human photopsin and rhodopsin, but is also excited by a far greater range of red light, even extending into the NIR in some species of freshwater fish. Porphyropsin is formed by opsin and 3,4-dehydroretinol, also called vitamin A2. In essence, we intend to completely cut vitamin A out of our diet and replace it with A2.
In order to provide valid scientific data for the community, we are adhering to a strict dietary regimen provided by the generous Mr. Rhinehart, the inventor of Soylent (www.soylent.me) and collecting data on visual spectrum shift changes via ERG. In order to purchase this equipment, we decided to crowdfund using the Microryza scientific research platform. We would greatly appreciate any financial assistance the community could offer this project--every dollar counts!!
All our results will of course be published free and open source following standardized research paper format, both on Microryza and on the publish.biohack.me page here. Our long-term goal, should this proof-of-concept experiment go well, is to develop a more permanent hack which inhibits vitamin A uptake and upregulates A2 uptake. The results of this later research will also be free and open source.
Here is our project page:
https://www.microryza.com/projects/can-we-biologically-extend-the-range-of-human-vision-into-the-near-infrared
Please feel free to ask any questions about the project or any suggestions to add to the project page here. Grind on!
Project members:
@glims --A2 production/sourcing; biochem
@Cassox -test subject; medical supervision
@Saal -test subject; shameless promotion; dead weight :P
@zombiegristle -test subject
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Comments
So is opsin basically rhodopsin minus the vitamin A? Or in other words, is the protein portion of photopsin/rhodopsin the same as porphyropsin when not complex with vitamin A/A2?
If they are the same protein( I'm not trying to rain on your parade), it would seem to me that there would at least be variations in the amino acid sequence between fish and humans that would change it's affinity from Vitamin A2 to Vitamin A.
I'm not sure if you guys would have the resources, but if you could get in touch with a local university or lab with the proper equipment, you could contract them to do a protein binding assay to determine if human opsin can complex correctly with vitamin A2. This in of itself would probably be worth publishing, but much slower than your current plan. On the other hand, it might be a bit more safe, seeing as if this doesn't work, you might end up being blind. No pain, no gain though right??? ;)
Another possible option would be if you can get your hands on genomic data for the
fish and compare the analogous protein amino acid sequence. Then you would be able to know for
sure (minus any post-translational conformational changes or epigenetic considerations).
Still, this is really cool and the DIYer in me says this has awesome potential if you succeed!
Don't misunderstand me; this certainly could be an issue but I doubt it. Opsins are pretty well conserved amongst chordates so the differences should be pretty slight.
@DOG_GOD: TBH, biochem isn't my specialty; that's more @glims and @Cassox. However, this experiment has been performed successfully several times on rodents, and we have reason to believe also by the US Navy on human subjects prior to the invention of the "snooperscope". I'm sure @glims can speak more to the porphyropsin binding process, but everything I've read on the subject indicates there's a high possibility of success.
besides, your brain would compensate for it, just as it white-balances.
Thanks for the answers! I see now that this really is quite feasible. Also, I just realized the difficulty of obtaining human opsin directly to do a binding assay lol. I guess there's always cadavers donated to science!
I'd love to hear any proposed ideas for getting around the membrane transporter issues regarding vitamin A2, if you're kicking them around. I suppose if you could get gene therapy to work, you could use the fish version of the vitamin A importer, though I would think the immune system would have something to say about a foreign protein on the cell membrane. Other than that, I have limited knowledge of how the vitamin A import protein functions; I found a pathway, but I'm not sure which one is the issue.
Is it RBP, CRALBP, IRBP, or CRBP or none of those?
Sorry for being confusing, on the microyza webpage there is mention of transport proteins having 4x the affinity for A1 compared to A2, I was just curious which transporter or proteins that this was referring to. I did some looking around and I came up with that graphic which is from webvision.med.utah.edu.
Thanks for the link though, I'll read through that paper before I ask any more confusing questions :)
We are actually going to be using ERG, electroretinograph. An ERG provides a simple yes/no answer to whether or not the photoreceptors are being stimulated. So a few electrodes are applied near the eye, and a type of contact lense electrode is applied directly to the eye. A cowling will prevent undesirable light from reaching the eye.
When a photostrobe in the near IR range is used to stimulate the eye, the ERG should then indicate whether or not the eye is senstive to this particular frequency. This way we can determine if there has been a shift in spectrum sensitivity, the degree of shift, and amplitude of response to the stimulation.
There is little doubt that A2 will be uptaken and used. If this is the case, it's still valuable because then there must be some difference in the human eye from pretty much all other species. Assuming A2 is bound by opsin, this doesn't automatically mean it's going to result in the visual change we want. In theory, we might find that we can't get the eyes to form enough porphyropsin via this method to affect a change we are conscious of. Reviewing previous studies though, I rather doubt this outcome. It's just a good policy to remain open to such factors.
I looked in a little to comparing protein sequences for Retinol Binding Protein on pBLAST and even between mice analogs and humans there was some amount of variability. I wanted to run a BLAST comparison for porphyropsin (fish) and rhodopsin (mammal), but I'm having some trouble finding fish opsin sequence. From what I can see though, they appear to be very conserved.
Another question, do fish and amphibians that use a porphyropsin system, use a differentiated form of RBP or another protein to import vitamin A2?
As mentioned in the paper, the only real difference between A1 and A2 is an extra ethylene in the paryene chain of A2, something that should have little to no effect on the protein regulatory process (at least in pigmentation; I can't speak to other functions authoritatively, but again should be negligible)
Also you may want to look into phyto chemical augmentations as it relates to gene expression. It could help achieve better results.