Session Q39: Physical Mechanisms of Membrane Remodeling

11:15 AM–2:15 PM, Wednesday, March 18, 2009
Room: 411

Sponsoring Unit: DBP
Chair: Markus Deserno, Carnegie Mellon

Abstract ID: BAPS.2009.MAR.Q39.2

Abstract: Q39.00002 : Membrane Disruption Effects of antimicrobial Peptide Protegrin-1

11:51 AM–12:03 PM

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  Hao Wang
    (Department of Chemistry, Emory University, Atlanta, Georgia 30322, USA)

  James Kindt
    (Department of Chemistry, Emory University, Atlanta, Georgia 30322, USA)

Molecular dynamics simulations have been performed to better understand membrane disruption induced by antimicrobial peptide Protegrin-1 (PG-1). Two distinct setups were adopted for atomistic simulations for DMPC/PG-1 systems. One started from bilayered ribbons either with or without the PG-1 peptides embedded and another one started from random lipid mixtures in the presence of the PG-1 peptides. Line tensions deduced from the ribbon simulations were generally lower with the PG-1 peptides embedded in ribbon edge, which supports edge-active role of the peptides. The random mixtures self-assembled into various structures. Extended simulations are being carried out to investigate the relation between concentration of the PG-1 peptides and the resultant structures. Furthermore, coarse-grained models have been used to simulate larger DMPC bilayers with the PG-1 peptides embedded. The PG-1 peptides were found to self-assemble into clusters. However, pore formation was not observed within our simulation period up to 3 microseconds. (DMPC: 1,2-Dimyristoyl-sn-Glycero-3-Phosphocholine)

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