SMAMP antimicrobial peptides

Al-Badri and co-workers [55] studied the effect of fine-tuning the cationic parameter of synthetic mimics of antimicrobial peptides (SMAMP) on haemolytic and antibacterial activities. A category of novel norbornene monomers that carry one, two or three Boc-protected amine-functionalities was synthesised (Figure 3.8). ROMP of the monomers, followed by deprotection of the amine groups led to cationic antimicrobial polynorbornenes that carry one, two and three charges per monomer repeat unit. It was observed that enhancing the number of amine groups on the most hydrophobic polymer effectively decreased its haemolytic activity. 

Keywords Antibacterial polymers Antimicrobial polymers Peptide analogs Peptidomimetics Polymer-membrane interaction Synthetic mimics of antimicrobial peptides, SMAMPs... 

Fig. 4 (a) Antimicrobial and hemolytic activity of three a,(3-peptides (1-3), compared to AMP magainin. (b) Axial view of predicted conformations of helical SMAMPs. Cationic residues are in red, hydrophobic residues are in black. SMAMP 1 is facially amphiphilic as an 11-helix (left column), SMAMP 2 is facially amphiphilic as a 14-helix (right column), and SMAMP 3 is facially amphiphilic in neither [65]... 

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