FIDELIO GERARDO DANIEL
Congresos y reuniones científicas
Título:
Interaction of antimicrobial peptides with POPC lipid structures modeled by coarse-grained molecular dynamics simulations
Autor/es:
BALATTI, GALO E.; MARTINI, M. FLORENCIA; AMBROGGIO E.E.,; FIDELIO G.D.,; PICKHOLZ, MÓNICA
Lugar:
San Miguel de Tucumán
Reunión:
Congreso; III LAFEBS, 9 Iberoamerican congress of Biophysics and XLV Annual Meeting of Argentinian Biophysical Society; 2016
Institución organizadora:
SAB
Resumen:
Antimicrobial Peptides (AMPs) are a wide group of small cationic
molecules of the innate immune system. They have proven activity
against agents among bacteria, fungi, viruses and eukaryotic parasites.
It is suggested that they act by binding to the bilayer increasing the permeability
of the membrane [1].
206
Poster Lipid-Protein interaction
Among them, two peptides obtained from australian tree frogs, the aurein
1.2 and the maculatin 1.2 show structural features typical of helical
AMPs with high lytic activity, the key aspect of AMPs [ibid]. Nevertheless,
is still under discussion the molecular mechanism by which they
damage biomembranes.
In order to shed light about the molecular mechanism of aurein and maculatin
interaction with membranes, we carried out extensive Molecular
Dynamics (MD) simulations. Taking into account the system size and
the time scales required, we have chosen a coarse grain approach within
the MARTINI force field [2].
The simulations were carried out starting from three different configurations:
the peptides placed in water near to a POPC planar bilayer
(?outside the membrane?), the peptides inside the hydrophobic core of
a POPC planar bilayer (?inside the membrane?), and the molecules randomly
distributed along the space (?self-assembly?). Our results show
that both peptides can form pore-like structures, highlighting two different
behaviors on the peptide-membrane interactions and membrane
leakage of aurein and maculatin, in good agreement with previous experimental
observations [1]. While maculatin can form a pore maintaining
the structure of the bilayer and can induce membrane curvature,
aurein exhibits surfactant properties and this may cause the total membrane
destabilization and disintegration.
References
1. E.E. Ambroggio, F. Separovic, J.H. Bowie, G.D. Fidelio, L.A. Bagatolli. Biophysical
Journal 89 (2005) 1874?1881.
2. X. Periole, S.J. Marrink. Methods in molecular biology 925 (2013) 533-565..
molecules of the innate immune system. They have proven activity
against agents among bacteria, fungi, viruses and eukaryotic parasites.
It is suggested that they act by binding to the bilayer increasing the permeability
of the membrane [1].
206
Poster Lipid-Protein interaction
Among them, two peptides obtained from australian tree frogs, the aurein
1.2 and the maculatin 1.2 show structural features typical of helical
AMPs with high lytic activity, the key aspect of AMPs [ibid]. Nevertheless,
is still under discussion the molecular mechanism by which they
damage biomembranes.
In order to shed light about the molecular mechanism of aurein and maculatin
interaction with membranes, we carried out extensive Molecular
Dynamics (MD) simulations. Taking into account the system size and
the time scales required, we have chosen a coarse grain approach within
the MARTINI force field [2].
The simulations were carried out starting from three different configurations:
the peptides placed in water near to a POPC planar bilayer
(?outside the membrane?), the peptides inside the hydrophobic core of
a POPC planar bilayer (?inside the membrane?), and the molecules randomly
distributed along the space (?self-assembly?). Our results show
that both peptides can form pore-like structures, highlighting two different
behaviors on the peptide-membrane interactions and membrane
leakage of aurein and maculatin, in good agreement with previous experimental
observations [1]. While maculatin can form a pore maintaining
the structure of the bilayer and can induce membrane curvature,
aurein exhibits surfactant properties and this may cause the total membrane
destabilization and disintegration.
References
1. E.E. Ambroggio, F. Separovic, J.H. Bowie, G.D. Fidelio, L.A. Bagatolli. Biophysical
Journal 89 (2005) 1874?1881.
2. X. Periole, S.J. Marrink. Methods in molecular biology 925 (2013) 533-565..
