University of British Columbia researchers have demonstrated that synthetic short tethered cationic antimicrobial proteins can be used to coat medical devices.
From the article intro in Chemistry and Biology:
Although many investigations of soluble antimicrobial peptides have served to establish the structure-activity relationships that dictate peptide antimicrobial activity and cytotoxicity, this is not the case for tethered antimicrobial peptides. Indeed, as immobilization of peptides to a surface would result in limitations to peptide mobility and thus the ability of peptides to enter into or translocate across membranes, it is imperative that structure-activity relationship investigations among tethered cationic antimicrobial peptides be established. Previously, we developed a high-throughput antimicrobial peptide activity screening assay utilizing Pseudomonas aeruginosa with a constitutively expressed luciferase (luxCDABE) gene cassette; however, this method was limited to free peptides in solution (Hilpert etal., 2005,Hilpert etal., 2006). Here we have adapted and made key modifications to this methodology to enable the identification of surface-bound peptides with antimicrobial activity using a high-throughput screening assay format. By creating a large library of peptides, we were able to investigate the influence of charged and hydrophobic residues on the antimicrobial activity of tethered peptides, as well as the influence of their positioning within the peptide sequence relative to the tethering surface. The resultant strategy will assist the development of peptidic antimicrobial surfaces that might exhibit certain advantages over those presently used in the clinic.
Full story: Using Nature’s Antibiotics to Coat Medical Devices
Paper in Chemistry & Biology…
