5 ms·
The peptide of interest has been named 'DRGN1' [1]. The actual full length DRG1 amino acid sequence of DRGN1 if you want to use it: PSKKTKPVKPKKVA As a genetic
by jfarlow 10y ago
The peptide of interest has been named 'DRGN1' [1]. The actual full length DRG1 amino acid sequence of DRGN1 if you want to use it: PSKKTKPVKPKKVA
As a genetically encoded peptide it has a few advantages over the traditional small molecule antibiotics you might know about from being prescribed by your doctor:
- It retains anti-biotic effect on gram-negative (hard to attack because they have a secondary wall) bacteria.
- It's mechanism of action is less well understood, but because it's not obviously just a 'signal jammer' than a small molecule antibiotic, developing resistance to anti-microbial peptides seems more difficult than with small molecules.
- It has anti-biofilm properties as well as well as anti-biotic properties (biofilms are a royal pain in hospitals - think catheters...)
- Anti-microbial peptides also often have a strange effect where they activate wound healing in non-microbes (people), rather than just being an ineffectively diluted poison or entirely benign (the way most small molecule antibiotics are).
- My favorite though, because it is genetically encodable, the anti-microbial properties can be conferred to other genetically encoded tools/machines/proteins. If you fuse the amino acid sequence to another protein's sequence, the new fusion protein will likely also have anti-microbial properties.
Spider silk gloves could have this peptide woven into them - and the R&D cost to at least try it out is likely a few hundred bucks and a day or two of effort, CRISPR could deliver a sequence that produces this peptide, or a protein that contained this peptide. The peptide could be produced at commercial scale attached to another 'filler protein' to coat stents/catheters to prevent biofilm buildup - adding exactly zero production cost if such a filler protein is already being used. Or fused to a protein that other 'good' bacteria already produce to prevent biofilm formation where it shouldn't be. Because it can be encodedly produced by nearly all life, it can be introduced genetically as a one-time cost/effort, letting the organism then produce the antibiotic, rather than having to mass-produce the antibiotic in some chemical reaction.
[0] The paper: https://www.nature.com/articles/s41522-017-0017-2 https://www.nature.com/articles/s41522-017-0017-2
[1] DRG1: https://serotiny.bio/notes/proteins/drgn1/ https://serotiny.bio/notes/proteins/drgn1/
- mkehrt 10y agoDoes the fact that it's a peptide mean it won't survive digestion and can't be taken orally?
- marcosdumay 10y agoOn a silver lining, this may mean that people won't give this thing to cattle and it won't accumulate on the wild. That may delay bacteria resistance.
- sndean 10y agoThis is one of the ways it's been sold. But, we've tried D-enantiomer peptides too, which aren't as readily degraded.
- TeMPOraL 10y agoDon't farmers ever inject stuff into cattle?
- marcosdumay 10y agoIt's more expensive. Farmers avoid injecting things in healthy cattle.
- arrosenberg 10y agoIt depends on the peptide and how it's affected by gastric acid. Some peptides can't be used at all, some can be modified so that the bioactive chemical is a result of digestion.
- drspacemonkey 10y agoJust to confirm, are you saying that this "miracle cure" news article (which are notoriously bullshit) might actually be true?
- folli 10y agoThe use cases are quite limited since it can only be applied externally (e.g. wound infections) and not against systemic infections.
- AstralStorm 10y agoEven there, there is quite a bit of potential for allergic reactions.
- jfarlow 10y agoIt's not a miracle cure, it's just a nicely different way of attacking a problem. It still has tradeoffs - I'm not versed on what they all are, but its tradeoffs are of a different kind than of small molecules. A few guesses of what those tradeoffs might look like: A peptide will be more expensive to synthesize in bulk, it will not have as long of a shelf-life, it likely has a different (not perfect) resistance mechanism and will be more or less effective on different specific microbes. It's likely not as effective on a per/molecule basis. And it's much larger, meaning it will have a greater difficulty diffusing through the body of an organism - and might actually be degraded more quickly once inside an organism because it's peptide-like. But the mere fact that there are alternative tools in our toolbox for different scenarios is useful in our fight against disease (if not a 'miracle'). DRGN1 is not the first of such antimicrobial peptides, but it was found in a systematic way, and once it was found it was systematically made more effective. This hints at workflows to mine and refine more genetically encoded peptides like it in the future.
- drspacemonkey 10y agoThank you very much for the insight!