Interaction of Antimicrobial Peptides with Bacterial Membrane

The antimicrobial peptides AMPs represent abundant and diverse group of molecules, which are evolved from many tissues and cells in the plant and animal kingdoms as protective reaction against infection organisms. They build a very strong rst line of innate immunity [1]. Despite their enormous variety, most AMPs work directly against microbes, through a mechanism involving membrane disintegration or/and formation of pores, which allows easier passage of the ions and the basic nutrients. Molecular mechanisms, and the way of penetration through the membrane can be var-ied to various peptides, depending on the sequence of amino acids, the lipid composition of the membrane and the concentration of peptides, but for the beginning of their action, they must rst be attracted to the bacterial surface. The objective of the present examination is namely the so called S-state, or an inactive state in which an AMP is oriented parallel before binding to the membrane. To this end we have conducted molecular dy-namics studies. The conformational changes in the quaternary structure of