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 a high rate of mutation, ends up changing one or more of its enzymes that are used to destroy the interface between a target protein and the antibiotic. In consequence, the antibiotic does not work.

But to adapt to a peptide antibiotic that makes a hole in the cell membrane is a different story. To protect itself, the bacterium would have to change the full composition of the cell membrane. 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 respond in minutes. Part of the reason for this quick response is how the peptide works on the cell membrane. But to destroy a cell, the peptide must also quickly find the bacterial membrane. How does this happen? The answer lies in the structure of the cell membrane. The plasmatic 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 possess a low negative electrical charge. On the other hand, a bacterial membrane is made up of 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 therapy of meningitis, a condition that affects 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 effective drugs.

But bringing a drug to clinical tests is time consuming and costly. It takes $300 million to bring a drug to market. This price covers every thing from discovery, identification, synthesis and clinical trials. This process can also take 10 or more years to accomplish.

Luckily we do not have to wait to obtain the benefits of antimicrobial peptides when it comes to combating acne or skin wounds, for they can be addressed with the peptides and proteins contained in the mucin of certain species of land snails, the same they use to repair their own tissues and calcium shell whenever damaged.

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