Natural antimicrobial agents could help to reduce infections, studies find

Published: 5-Mar-2013

Researchers look at properties of proteins and peptides from human saliva and fish gills


Antimicrobial agents from living beings could help to reduce infections, according to the findings of two research projects carried out by researchers in the US.

In the first project, a team from Boston University is using a genetically engineered variant of the histatin 3 protein found in human saliva to reduce Candida infections, while the other project, by a team at Worcester Polytechnic Institute in Massachusetts, is applying the antimicrobial peptides found in fish gills to kill E. coli pathogens.

The Boston study, Anti-candidal activity of genetically engineered histatin variants with multiple functional domains, published in the online journal, PLoS One, demonstrated that duplicating active functional domains in the amino acid sequence could enhance their antifungal properties. Histatin preparations have already demonstrated their effectiveness in reducing Candida infections in AIDS patients. Antibacterial and antifungal mouthwash is one possible application. Genetically enhanced histatins could also be used to address skin infections.

Histatin preparations have already demonstrated their effectiveness in reducing Candida infections in AIDS patients

Meanwhile, the Worcester Polytechnic Institute team hopes to adapt the fish gill antimicrobial peptide to create bacteria-killing surfaces. Such surfaces may help reduce healthcare-acquired infections. Fish have evolved powerful defences, including the antimicrobial peptide Chrysophsin-1 to trap and kill water-borne pathogens before they enter the bloodstream.

The study, Creating Antibacterial Surfaces with the Peptide Chrysophsin-1, published in ACS Applied Materials & Interfaces, is part of the team’s effort to understand the biochemical mechanics of the pathogen-trapping process.

Using two different methods to attach the peptide to silicon and gold surfaces, the researchers then measured how well the bound peptides killed E. coli, a bacterial pathogen. When the peptides were absorbed directly into the gold and silicon crystals, and thus were lying flat on the surface, they killed 34% of the culture’s bacteria. However, when the peptides were glued so that the peptides seemed to be standing on their ends, they killed 82% of the bacteria.

Next on their research agenda is to adapt the process to materials such as titanium, stainless steel, and plastic, which are commonly used in food preparation and healthcare.

The peptide Chrysophsin-1, found in fish gills, is being studied for its antimicrobial properties and possible role in infection reduction in healthcare settings.

You may also like