In an article published in Plos One, researchers from INRS-Institut Armand-Frappier Research Centre reported a strategy that could lead to the discovery of new cationic antimicrobial peptides (CAMPs) with greatly enhanced antimicrobial properties. The peptide modified for the study retained considerable activity against biofilms responsible for increasing the severity of various infections. The strategy thus holds promise for combatting multidrug resistant bacteria. For the purpose of the study, the researchers selected a peptide--pep1037--already known for its antimicrobial potential and antibiofilm activity against Pseudomonas aeruginosa and Burkholderia, two pathogens responsible for serious complications in individuals with cystic fibrosis. The peptide was modified by adding a cysteine to the end to generate a dimer. The antimicrobial activity of the new molecule was 60 times greater than that of the original peptide. ‘Although there are currently no clinically approved antimicrobials that target bacterial biofilms, an estimated 80% of all bacterial infections have a biofilm component.’ "Our results show that the dimer is of significant interest because it has a dual potential to inhibit both bacterial and biofilm growth. It could potentially be used for therapy in combination with clinically relevant antibiotics," explained the authors of the study. Although there are currently no clinically approved antimicrobials that target bacterial biofilms, an estimated 80% of all bacterial infections have a biofilm component. These infections are much more difficult to eradicate because they are 10-1,000 times more resistant to antibiotic treatment. The formation of biofilms is associated with severe antibiotic resistance in the lungs of patients with cystic fibrosis, among others. To date, very few studies have reported on the effect of dimerizing cationic antimicrobial peptides by adding a cysteine, especially at the specific location modified by the researchers, i.e., at the end. The results obtained pave the way to improving this class of antibiotics, which occur naturally in many organisms. Source: Eurekalert << NHRC Issues Notice to Delhi Government Over Contaminated Ey... Shoulder Pad Foam Layer Plays Role in Fewer Concussions >> Recommended Reading New Class of Peptides Discovered from Bacteria Helps to Kill Insect Larva A new class of rhabdopeptide or xenortide peptides from photorhabdus and xenorhabdus bacteria was found to infect and kill insect larva. READ MORE Next Generation of Shuttle Peptides to Target the Brain The administration of drugs to the brain is one of the main challenges of drug development, given the significant number of patients with neurological diseases. READ MORE Brushing Up Peptides Boosts Their Potential by Helping Them to Get Inside Cells The versatility of the new method allows modification of peptides and could enable the development of peptide based drugs to treat a broad range of illnesses. READ MORE UV Light Used for In-vivo Activation of Disguised Peptides Researchers used ultraviolet light onto the molecules through the skin to sneak biomaterials containing peptide signaling molecules into living animals. READ MORE Food Preservatives - How Safe Are They? Food preservatives are basically antimicrobials or anti-oxidants that help preserve food by destroying the microbes and stopping decomposition of food products. READ MORE Most Popular on Medindia Fongitar (Zinc Pyrithionone) Daily Calorie Requirements How to Reduce School Bag Weight - Simple Tips More News on: Food Preservatives - How Safe Are They?