arrow
Volume 11, Issue 3
How the Antimicrobial Peptides Kill Bacteria: Computational Physics Insights

Licui Chen, Lianghui Gao, Weihai Fang & Leonardo Golubovic

Commun. Comput. Phys., 11 (2012), pp. 709-725.

Published online: 2012-11

Export citation
  • Abstract

In the present article, coarse grained Dissipative Particle Dynamics simulation with implementation of electrostatic interactions is developed in constant pressure and surface tension ensemble to elucidate how the antimicrobial peptide molecules affect bilayer cell membrane structure and kill bacteria. We find that peptides with different chemical-physical properties exhibit different membrane obstructing mechanisms. Peptide molecules can destroy vital functions of the affected bacteria by translocating across their membranes via worm-holes, or by associating with membrane lipids to form hydrophilic cores trapped inside the hydrophobic domain of the membranes. In the latter model, the affected membranes are strongly buckled, in accord with very recent experimental observations [G. E. Fantner et al., Nat. Nanotech., 5 (2010), pp. 280-285].

  • Keywords

  • AMS Subject Headings

  • Copyright

COPYRIGHT: © Global Science Press

  • Email address
  • BibTex
  • RIS
  • TXT
@Article{CiCP-11-709, author = {Licui Chen, Lianghui Gao, Weihai Fang and Leonardo Golubovic}, title = {How the Antimicrobial Peptides Kill Bacteria: Computational Physics Insights}, journal = {Communications in Computational Physics}, year = {2012}, volume = {11}, number = {3}, pages = {709--725}, abstract = {

In the present article, coarse grained Dissipative Particle Dynamics simulation with implementation of electrostatic interactions is developed in constant pressure and surface tension ensemble to elucidate how the antimicrobial peptide molecules affect bilayer cell membrane structure and kill bacteria. We find that peptides with different chemical-physical properties exhibit different membrane obstructing mechanisms. Peptide molecules can destroy vital functions of the affected bacteria by translocating across their membranes via worm-holes, or by associating with membrane lipids to form hydrophilic cores trapped inside the hydrophobic domain of the membranes. In the latter model, the affected membranes are strongly buckled, in accord with very recent experimental observations [G. E. Fantner et al., Nat. Nanotech., 5 (2010), pp. 280-285].

}, issn = {1991-7120}, doi = {https://doi.org/10.4208/cicp.071210.240511a}, url = {http://global-sci.org/intro/article_detail/cicp/7387.html} }
TY - JOUR T1 - How the Antimicrobial Peptides Kill Bacteria: Computational Physics Insights AU - Licui Chen, Lianghui Gao, Weihai Fang & Leonardo Golubovic JO - Communications in Computational Physics VL - 3 SP - 709 EP - 725 PY - 2012 DA - 2012/11 SN - 11 DO - http://doi.org/10.4208/cicp.071210.240511a UR - https://global-sci.org/intro/article_detail/cicp/7387.html KW - AB -

In the present article, coarse grained Dissipative Particle Dynamics simulation with implementation of electrostatic interactions is developed in constant pressure and surface tension ensemble to elucidate how the antimicrobial peptide molecules affect bilayer cell membrane structure and kill bacteria. We find that peptides with different chemical-physical properties exhibit different membrane obstructing mechanisms. Peptide molecules can destroy vital functions of the affected bacteria by translocating across their membranes via worm-holes, or by associating with membrane lipids to form hydrophilic cores trapped inside the hydrophobic domain of the membranes. In the latter model, the affected membranes are strongly buckled, in accord with very recent experimental observations [G. E. Fantner et al., Nat. Nanotech., 5 (2010), pp. 280-285].

Licui Chen, Lianghui Gao, Weihai Fang and Leonardo Golubovic. (2012). How the Antimicrobial Peptides Kill Bacteria: Computational Physics Insights. Communications in Computational Physics. 11 (3). 709-725. doi:10.4208/cicp.071210.240511a
Copy to clipboard
The citation has been copied to your clipboard