Bacteria have survived for millions of years by developing resistance to new aggressors including biological antibiotics like penicillin. What simply occurs is that the bacteria, with an elevated rate of mutation, ends up modifying one or more of its enzymes that are used to break the interface between a target protein and the antibiotic. In consequence, the antibiotic does not work.

But to respond to a peptide antibiotic that makes a hole in the cell wall is a different story. To defend itself, the bacterium would have to change the entire composition of the cell wall. And to change the composition of a membrane would imply changing many of the enzymes that are responsible for making the intricate membrane in the first place.

Peptide antibiotics act within minutes. Part of the reason for this quick response is how the peptide works on the cell wall. But to destroy a cell, the peptide must also quickly find the bacterial wall. How does this occur? The answer lies in the construction of the cell membrane. The plasmatic wall of eukaryotic cells is much different than the wall of a prokaryotic cell. Eukaryotic cell walls are made of a phospholipid bilayer and cholesterol. Consequently, these walls possess a low negative electrical charge. On the other hand, a bacterial wall is made up of fats and sugars. This difference in construction means that bacteria have an elevated negative electrical charge that quickly attracts the peptide antibiotics.

Health Benefits

Peptide antibiotics are efficient. In one medical trial for the therapy of meningitis, a disease that attacks 3,000 children a year, a peptide antibiotic not only killed the bacterium which secretes the toxin, but it also bound to the toxin preventing the damage the endotoxin inflicts. This is a promising new venue for research, and creating efficient drugs.

But bringing a drug to medical trial is time consuming and expensive. It takes $300 million to bring a drug to public. This cost 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 obtain the benefits of antimicrobial peptides when it comes to fighting acne or skin injuries, for they can be treated with the peptides and proteins contained in the mucin of certain 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 efficient 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 importantly increased by acne infection.

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