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Antimicrobial peptides are small molecules made up of amino acids that act against microbes. They could provide alternative forms of treatment as more microorganisms become resistant to antibiotics. There are over 800 types of antimicrobial peptides, and they attack microorganisms by changing their cell membrane. Synthetic versions of histatins have shown potential in treating infections. However, relatively few have been developed and tested, and they often appear less effective in clinical trials. Antimicrobial peptides are not harmful to human cells and are not associated with the development of resistance in the way that antibiotics are.
An antimicrobial peptide, or host defense peptide, is part of the innate immune system that is present from birth to protect the body from infection. Structurally, it is a small molecule made up of a chain of amino acids, the units from which proteins are made. There are several types of antimicrobial peptides and they are found in all living creatures, where they act against microbes such as bacteria and viruses. As more microorganisms become resistant to antibiotics, it is thought that the use of antimicrobial peptides could provide alternative forms of treatment. Potentially, customized peptides could be made to treat infections, boost the immune response and neutralize toxins produced by microbes.
The antimicrobial peptide molecule consists of a chain of amino acids, ranging in length from six to 100 units. Over 800 different types of antimicrobial peptides have been recognized. They were divided into four main classes based on their overall shape. These classes are known as α-helical, sheet-sheet, extended, and ring peptides. The most common types of human peptides are histatins, which are found in saliva, and defensins and cathelicidins, which are produced by cells of the immune system.
In most cases, an antimicrobial peptide attacks a microorganism by changing its cell membrane. Holes are created in the membrane that allow important substances such as nutrients to flow out of the cell. While the details are not fully understood, it is thought that there are different membrane modification mechanisms used by different types of peptides.
Research involving synthetic versions of histatins has shown that they can act against the yeast known as Candida albicans. This suggests that artificial histatins could be used to treat the yeast infection known as candidiasis affecting the mouths of HIV-infected patients. Other research has suggested that histatins might be effective in treating certain bacterial infections that occur in burns and skin wounds.
Thousands of different types of antimicrobial peptides could be produced to treat a variety of infections, but relatively few have been developed and tested so far. One problem has been that, in clinical trials involving patients, antimicrobial peptides often appear less effective than they appear when tested in the laboratory. Another disadvantage is that synthetic antimicrobial peptides are expensive to produce. Advantages of developing antimicrobial peptides as drugs include that they are not harmful to human cells and are not associated with the development of resistance in the way that antibiotics are.
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