مهشید دانش شهرکی - ۱دانشگاه تحصیلات تکمیلی زنجان
سارا محمدی نژاد - ۲تحصیلات تکمیلی زنجان
سهیلا امامیاری

Antimicrobial peptides are essential components of innate immunity system that can be found in living organisms. These small cationic peptides provide a natural defense against various pathogens [1].Nowadays AMPs are so important because they are considered as a potential alternative of antibiotic because of its ability to circumvent bacterial resistance [2]. One well-known AMP is Cathelicidin which is expressed in epithelial cells and in leukocytes such as monocytes, neutrophils, T cells, NK cells, and B cells. Cathelicidin is small, cationic peptide that possesses broad-spectrum antimicrobial activity. LL-37, the only human cathelicidin, is a 37-residue, amphipathic, helical and cationic (+6) peptide [3]. computational modeling plays considerable role in knowing atomistic activity of AMPs [4]. These peptides primarily act on the first line of defense of bacteria and cause bacterial death [5]. computational approaches have tried to understand this mechanism of action, that is, how the AMPs interact with the bacterial membrane. In this study, we are going to investigate the interactions between LL-37 and dipalmitoylphosphatidylcholine bilayer by use of Umbrella sampling simulations. We pulled LL-37 close to the membrane in two vertical and horizontal direction and calculated the free energies after drawing the PMF (potential of the mean force) curves.

Antimicrobial peptides; Cathelicidin; Host defense peptide; DPPC; LL,37