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 ( 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 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:

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



  • Argh! I'd love to fund the project. Unfortunately, I haven't gotten around to setting up online monetary resources (Like paypal) yet. You might want to supply an address we can send checks and cash to.

    Very excited to see what this experiment yields. 
  • take bitcoins?
  • Sorry dude, this straight laced web funding project only takes plastic.

    @TheGreyKnight - we take straight up credit cards. no need to get all paypal'd
  • Awesome, glad to see this actually happening. I am really curious about the practicality of this project. Pledged $50. 
  • Thanks, @meanderingman! Please let us know if you see anything that could be improved on the project page or have any questions about the project
  • we launch Monday!
    everyone come and check it out. even one buck helps :)

    these bold grinders are ready to brute force hack their metabolic pathways to bring you the latest in cool body science.

    All progress will be open source and accessible to the community.

  • Awww yeah, I'm bold! O.o
  • Do you need any more test subjects?
  • Interesting concept Saal, a few quick questions though.

    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!
  • Actually, that was a preliminary question that's been answered via a different route. Although there certainly could be variation in the structure of the proteins in comparison to that in fish, all that really matters is whether or not mammalian retinal cells can form Porphyropsin. There have been a plethora of animal studies performed ranging rats to bird and it seems like a pretty universal occurrence.
    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.
  • @begonia: I'm sorry, but we've already budgeted for 3 subjects & it's a bit late to add another person to the protocol. You're more than welcome to all the research we've gathered, however, and I see no reason why you couldn't do this yourself individually. Although you might want to let us guinea pig it first anyway, as @DOG_GOD is absolutely correct; this experiment carries a risk of blindness, among other things up to and including death.

    @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.
  • I feel that the protein question was already answered well enough, though if there are any other questions, please let me or anyone else in the know. we need as much stress testing as we can get from you guys so that we have the most robust and solid project that we can have.

    Just a quick note. blindness caused by this experiment is reversible. to get to the point where you have xerophthalmia and your eye sight is totally jacked, well, it's outside the timeline of this project.

    @DOG_GOD  excellent questions and ideas. having another project lined up is crucial to continued research. i will talk with some of my associates in other labs and see if i can get a protein binding assay set up. We wont be able to do it until we have our molecule but it shouldn't take long after that.  while i don't think that it would be super paper worthy (or at least, not nature level. there have been, as mentioned, a number of works on this process) it could be a solid reference paper and great background work for what we are doing.

    @begonia, as @Saal mentioned, all of the work with be accessible to the community and open source. functional protocols will be posted here as well as other locations. sorry we can't test on you directly ;)
  • I was volunteering for the study specifically. If you are full on guinea pigs, I'll let you all test it out first before I try. It is an interesting study, and I look forward to hearing the results. 
  • I've been promoting your project and will be getting hit with a slew of questions. Here is the first: 

    "Here's the problem: your own body heat flows from your head through your sclera and into your eyeballs and fills them with infrared light. If you could cool your sclera and optic nerve down to room temperature, then the ability to see IR light might be useful. Otherwise, you're just adding a red haze to everything that you see."

    Do you want questions directed here, or elsewhere?
  • @DirectorX , hm. that shouldn't be a concern. your body temperature won't contribute a noticeable ammount of IR radiation in the targeted spectrum. unless your body temperature reaches pretty high temperatures (way past the boiling point of water). in such a case you really have other things to worry about than a bit purpleish/redish tinting of your vision.
    besides, your brain would compensate for it, just as it white-balances.
  • Go ahead and direct questions here. Any way that we can help you answer questions sounds good to me.

    Looks like @ThomasEgi  pretty much nailed that one. Remember that the wavelengths for thermal radiation and (near or normal) infrared radiation are totally different in size. Seeing infrared is not the same things as seeing heat.
  • Actually, that was a question I directed to @Cassox when I first read his blog post on the subject, well before we started seriously working on making this happen. The heat radiation emitted from the sclera is well outside our target visual spectrum.
  • edited September 2013
    @Cassox and @glimms and @Saal:

    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?
  • Can you clarify your question please?
    RBP is i believe the one you are talking about. however, my research also shows to others that aren't shown on this graphic ABCA4 and STRA6 that are very crucial. what is the context of your graphic and could you be more clear about the membrane transporter issues you are referring to?

    i have added a new paper to the library called " Membrane receptors and transporters involved in the function and transport of vitamin A and its derivatives". this will give you some background on the topic.
  • @glims

    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

    Thanks for the link though, I'll read through that paper before I ask any more confusing questions :)
  • ah, that's what you meant by the transport protein issues. Retinol Binding Protein (RGB) is the main one. Altering that pathway is a complicated process as i believe both A1 and A2 utilize it. while there ways of inhibiting some of the proteins involved in the transportation, the systemic effects all tend to look really grim. @Cassox has done a lot of reading about this.
  • Out of curiosity, what kind of data do you expect to be getting from the EEG readers? I wasn't aware that you could get useful info about vision from them. Are you using them in combination with some other sensors? 
  • edited September 2013

    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. image

    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.

  • Interesting paper @glims, thanks for the background.

    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? 

  • @DOG_GOD: I'll see if I can find a metabolic pathway for a freshwater fish that utilizes the porphyropsin visual system. In the meantime, here's another paper you might like to have a go at:

    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)
  • Will your study be monitoring the entire visible spectrum, or just infrared sensitivity? If this shows a positive shift toward the infrared, I'd be curious to know whether the test subjects detect any decrease in violet sensitivity.
  • will be measuring just the infrared. the lowered re activity to blue light is most likely expected. if you plot the absorbency of the two proteins you get two staggered bell curves. just as with anything else, when you move into a different part of the em spectrum, you generally leave the opposite side.
  •  Some research i found regarding this. Not sure if you guys have seen or not so thought I'd post just in case. 
    Also you may want to look into phyto chemical augmentations as it relates to gene expression. It could help achieve better results. 
  • Funny Enough, that source was authored by our very own @Cassox ;

    And possibly for the future, you should see if you can find a way of enhancing the vitamin A2 uptake with chemicals or other processes, so that it isn't necessary to totally eliminate standard vitamin A from your diet.
  • we are looking into ways to not have to mess with the diet. this current project is our proof of concept, the step beyond the blog post where we can say "hey, this works, can we have more research money now"

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