Molecular Dynamics Simulations of Interaction between Indolicidin and an Asymmetric Membrane

Authors

  • Peicho Petkov University of Sofia "St. Kliment Ohridski" Faculty of Physics Atomic Physics Department
  • Rositsa Marinova* University of Sofia "St. Kliment Ohridski" Faculty of Physics Atomic Physics Department
  • Leandar Litov University of Sofia "St. Kliment Ohridski" Faculty of Physics Atomic Physics Department

DOI:

https://doi.org/10.11145/462

Abstract

Antimicrobial peptides (AMPs) are a component of the innate immune system. TheyВ areВ  small proteins with broad spectrum antimicrobial activity against bacteria,В viruses and fungi. As such, they must interact with pathogenic membranes, eitherВ through translocation or by disrupting their structural integrity [1]. ToВ understand how this peptides permeabilize bacterial membrane, we performedВ coarse-grained simulation, using MARTINI force field. We studied the interactionВ between the 13-residue cationic peptide indolicidin, isolated from cytoplasmicВ granules of bovine neutrophils with different types of membranes. Indolicidin isВ an intensively studied antimicrobial peptide. This very efficient antimicrobialВ agent is the shortest natural AMPs and has a large proportion of tryptophanВ residues (39%) of any known protein. Furthermore, it exhibits activity againstВ Gram-positive and Gram-negative bacteria, but it does not lyse the bacterialВ cells [2]. В We investigated indolicidin interactions with both symmetric and asymmetricВ bilayers consisting of POPE and POPG lipids. In the former case, the peptideВ penetrate the membrane, but in the latter this process is faster and it inducesВ reorganization of the bilayer, after forming a pore and crossing the membrane.В We also examined the effect ofВ  indolicidin concentration on the morphology ofВ the membrane.

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Published

2015-04-23

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Conference Contributions