Bacteria have survived for millions of years by creating resistance to new stressors including biological antibiotics like penicillin. What simply occurs is that the bacteria, with an elevated rate of variability, ends up changing 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 punches a hole in the cellular membrane is a different story. To protect itself, the bacterium would have to change the entire 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 quick response is how the peptide works on the cellular 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 plasma membrane of eukaryotic cells is much different than the membrane of a prokaryotic cell. Eukaryotic cell walls are made of a phospholipid bilayer and cholesterol. Consequently, these walls have 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 an elevated negative electrical charge that promptly 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 trial is time consuming and expensive. It takes $300 million to bring a drug to public. This price covers 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 combating acne or skin wounds, for they can be treated with the peptides and proteins included in the mucin of certain species of land snails, the same they produce to repair their own tissues and calcium shell whenever damaged.

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