This review article provides a good overview of different AMPs and the history of their discovery: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3873676/
"It punched holes in the outer membranes of both gram-negative and gram-positive bacteria, it dissolved the biofilms that glue bacteria together, and it sped skin healing."
Getting through the cell walls of gram-negative bacteria alone would make this worth investigating, but the other two added to it are like icing on the life-saving cake.
If the question is "Is this the greatest antibiotic ever", well, sure you'll want to compare it against a slew of other compounds. But if your question is "does this increase the speed of healing at all?" as a first test before later, more complex experiments, then this seems fine to me.
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.
 The paper: https://www.nature.com/articles/s41522-017-0017-2
 DRG1: https://serotiny.bio/notes/proteins/drgn1/
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.
>Bacteriophage therapy, the use of viruses that infect bacteria as antimicrobials, has been championed as a promising alternative to conventional antibiotics. Although in the laboratory bacterial resistance against phages arises rapidly, resistance so far has been an only minor problem for the effectiveness of phage therapy. Resistance to antibiotics, however, has become a major issue after decades of extensive use. Should we expect similar problems after long-term use of phages as antimicrobials? Like antibiotics, phages are often noted to be drivers of bacterial evolution. Should we expect phage-treated pathogens to develop a general resistance to phages over time, a resistance against which only, for example, hypothetically co-evolved phages might be infective? Here we argue that the global infection patterns of phages suggest that this is not necessarily a concern as environmental phages often can infect bacteria with which those phages lack any recent co-evolutionary history.
Interesting to learn that the "bite and sepsis" theory was debunked-ish years ago.
Also interesting to learn that they're hard to study? It surprises me that such a well-known species is still that opaque, and the article gives some hints as to why.
edit: Huh - after getting curious it looks like the above is precisely my 'incongruent expectation'. From this article in 2001 about antimicrobial histone peptides found in salmon :
"Most antimicrobial activity is an extracellular event or occurs in the cellular lysosomal compartment. Therefore, an in vivo antimicrobial role for salmon histone H1 might seem incongruent with this protein’s assumed nuclear location and nucleosomal role. In mammals, however, histone H1 has been found outside the nucleus. It is present in the cytosol of human intestinal villus cells, from which it is released into the intestinal lumen during normal cell sloughing. Histone H1 is also found on the surfaces of murine macrophages where it serves as a receptor for thyroglobulin and it is a cell surface protein in murine neurons and in human monocytes. Therefore, histone H1 is not limited to the nucleus in all cells and it may be released to locations where it can act as an extracellular antimicrobial agent. Moreover, an antimicrobial role has been proposed for histone H1."
 (2001) http://www.sciencedirect.com/science/article/pii/S0006291X01...
> I'm not sure it is an 'of course' here - rather it might actually be a lucky find while playing with the truly cool sounding 'dragon's blood'.
It's most likely a result of the method used to pick peptides out of the blood samples . Histone peptides have lots of K/Rs, and the bait used to trap the peptides is tuned to pull out small peptides with >5+ (? IIRC) net positive charge. So, pretty sure it's a lucky find while sifting through lots of histone peptides, where something inhibits/degrades biofilm formation and helps wounds close.
“I wouldn’t turn down wild dragon blood if it was sent to me and I thought it was collected ethically,” Dr. Bishop said. “But I’m not going to go out in the wild to try to get it.”
Why the different attitude towards mice and guinea pigs?
Not that researchers collect their mice from the wild...
Disappearing ecosystem threaten directly humanity: food, water, even climate.
That's just the tip of the iceberg though. A lot of innovation are still coming from nature. We rely on solution already found by millions of years of evolution to solve our problem. Short of AI singularity, there is no substitute.