Bacteria have survived for millions of years by developing 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 destroy the link between a target protein and the antibiotic. As a result, the antibiotic does not work.
But to respond to a peptide antibiotic that punches a hole in the cell wall is a different story. To protect itself, the bacterium would have to change the full composition of the cellular 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 within minutes. Part of the reason for this quick response is how the peptide acts on the cellular membrane. But to kill 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 walls 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 made up of fats and sugars. This difference in construction implies that bacteria have a high negative electrical charge that promptly attracts the peptide antibiotics.
Health Benefits
Peptide antibiotics are efficient. In one medical trial for the therapy of meningitis, a condition that afflicts 3,000 children a year, a peptide antibiotic not only killed the bacterium which produces the toxin, but it also bound to the toxin preventing the harm the endotoxin produces. This is a promising new venue for research, and creating effective drugs.
But bringing a drug to medical 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 can also take 10 or more years to accomplish.
Luckily we do not have to wait to get the benefits of antimicrobial peptides when combating acne or skin wounds, for they can be addressed with the peptides and proteins contained in the mucin of some species of land snails, the same they produce to repair their own body and calcium shell whenever damaged.
The biological action of the snail's mucin is very effective against skin 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 mediators (i.e. interleukin-6, hydrogen peroxide, histamines, bacterial toxins) that are importantly increased by acne infection.
You can now get rid of scars and various kinds of dermal conditions thanks to a new skin care solution elaborated with biological ingredients that rejuvenate your skin without leaving undesired side effects.
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