Simulations Suggest Possible Novel Membrane Pore Structure

Investor logo
Investor logo

Warning

This publication doesn't include Faculty of Sports Studies. It includes Central European Institute of Technology. Official publication website can be found on muni.cz.
Authors

VÁCHA Robert FRENKEL D.

Year of publication 2014
Type Article in Periodical
Magazine / Source Langmuir
MU Faculty or unit

Central European Institute of Technology

Citation
Web http://pubs.acs.org/doi/abs/10.1021/la402727a
Doi http://dx.doi.org/10.1021/la402727a
Field Physical chemistry and theoretical chemistry
Keywords MOLECULAR-DYNAMICS SIMULATIONS; ANTIMICROBIAL PEPTIDES; STATE NMR; BILAYER-MEMBRANES; LIPID-BILAYERS; AMYLOID PORES; ION CHANNELS; FORCE-FIELD; MODEL; DISEASE
Description Amphiphilic proteins and peptides can induce the formation of stable and metastable pores in membranes. Using coarse-grained simulations, we have studied the factors that affect structure of peptide-stabilized pores. Our simulations are able to reproduce the formation of the well-known barrel-stave or toroidal pores, but in addition, we find evidence for a novel "double-belt" pore structure: in this structure the peptides that coat the membrane pore are oriented parallel to the membrane plane. To check the predictions of our coarse-grained model, we have performed more detailed simulations, using the MARTINI force field. These simulations show that the double-belt structure is stable up to at least the microsecond time scale.
Related projects:

You are running an old browser version. We recommend updating your browser to its latest version.

More info