Lipid selectivity in novel antimicrobial peptides: implication on antimicrobial and hemolytic activity

MATURANA, PATRICIA; SANTOS, NUNO; MAFFIA, PAULO; HOLLMANN, AXEL

Tucumán

Congreso; XLV Reunión Anual de la Sociedad Argentina de Biofísica, Santiago del Estero; 2016

Sociedad Argentina de Biofisica (SAB)

Cationic antimicrobial peptides (CAMPs) represent important self defense molecules in many organisms, including humans. These peptides have a broad spectrum of activities, killing or neutralizing many Gram- and Gram+ bacteria. The emergence of multidrug resistant microbes has stimulated research on the development of alternative antibiotics. For a peptide to be considered for therapeutic development, it needs to not only possess potent antimicrobial activity but also have low toxicity to human cells. We designed two novel peptides, peptide p6 (GLLWKWGWKWKEFLRIVGY) that resulted with high hemolytic values and poor antimicrobial activity and peptide p6.2 (GLLRKWGKKWKEFLRRVWK) derived from the previous one, with lower hemolysis and dramatically increased antimicrobial activity.The main point of this work was to establish a correlation between membrane affinity and antimicrobial or hemolytic activity, in this context we choose two lipid formulations, pure DMPC as PC is mainly contained in mammalian membranes and DMPC:DMPG 5:1 as a simplified model of bacterial membranes.