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Bacteria have survived for millions of years by creating resistance to new stressors including biological antibiotics like penicillin. What simply happens is that the bacteria, with a high rate of variability, ends up modifying one or more of its enzymes that are used to break the link between a target protein and the antibiotic. As a resulting, the antibiotic does not work.

But to respond to a peptide antibiotic that punches a hole in the cellular membrane is a different story. To protect itself, the bacterium would need to change the full composition of the cellular membrane. And to change the composition of a membrane would mean changing several of the enzymes that are responsible for making the complex membrane in the first place.

Peptide antibiotics respond within minutes. Part of the reason for this rapid response is how the peptide acts on the cellular membrane. But to destroy a cell, the peptide must also quickly find the bacterial membrane. How does this occur? The answer lies in the structure of the cell membrane. The plasma membrane of eukaryotic cells is much different than the membrane of a prokaryotic cell. Eukaryotic cell membranes are constructed of a phospholipid bilayer and cholesterol. Consequently, these membranes have a low negative electrical charge. On the other hand, a bacterial membrane is filled with fats and sugars. This difference in construction means that bacteria have a high negative electrical charge that quickly attracts the peptide antibiotics.

Health Benefits

Peptide antibiotics are effective. In one clinical trial for the treatment of meningitis, a condition that affects 3,000 children a year, a peptide antibiotic not only killed the bacterium which produces the toxin, but it also bound to the toxin avoiding the damage the endotoxin produces. This is a promising new venue for research, and creating effective drugs.

But bringing a drug to clinical trial is time consuming and expensive. It takes $300 million to bring a drug to public. This price includes every thing from discovery, identification, synthesis and clinical trials. This process may also take 10 or more years to accomplish.

Fortunately we do not have to wait to get the benefits of antimicrobial peptides when it comes to fighting acne or skin injuries, for they can be addressed with the peptides and proteins included in the mucin of some species of land snails, the same they use to repair their own body and calcium shell whenever damaged.

The biological action of the snail's mucin is highly effective against dermal infections and acne inflammation, and without the pitfalls of pharmaceutical antibiotics or the secondary effects of harsh chemicals. The mucin also aids to get rid of the chemical inflammatory promoters (i.e. interleukin-6, hydrogen peroxide, histamines, bacterial toxins) that are significantly increased by acne infection.

This type of treatment can be the ultimate biological skin product to deal with something as unnoticeableas an acne scar to something as damaging as a burn scars.