ε-Peptide Chimeras as Novel Antimicrobials
The prevalence of antibiotic resistance of bacterial pathogens requires development of new antibacterials to overcome this limitation. Our previous work has demonstrated that cationic antimicrobial peptides with unusual architecture are often resistant to proteolytic degradation . An example is a cascade-type of dendrimeric peptide (RLYR)4K2K that shows high in vitro antibacterial activity. It contains a trilysine core (K2K) that radiates four tetrapeptide RLYR arms with its sequence derived from the repeating topological motif of a known and potent antimicrobial peptide, protegrin-1 .
Here we report our continuing effort in developing new antimicrobial peptides with novel branched architecture using the s-amine of lysine for the ε-peptide backbone and functionalized α-amines as pendant side chains to give a branched α,ε-peptide containing two RLYR motifs. Since ε-peptides are found naturally as poly-ε-lysines which are generally stable to proteolytic enzymes, but...
KeywordsAntimicrobial Peptide Radial Diffusion Cationic Antimicrobial Peptide Extended Strand Straight Forward Manner
The work was in part supported by US public Health Service NIH Grant EB001986.