Investigation of antibacterial activity of LL-37 using umbrella sampling simulation
Publish place: Eighth Bioinformatics Conference of Iran
Publish Year: 1397
نوع سند: مقاله کنفرانسی
زبان: English
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شناسه ملی سند علمی:
IBIS08_054
تاریخ نمایه سازی: 9 مرداد 1398
Abstract:
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.
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