INVESTIGADORES
ENRIZ Ricardo Daniel
artículos
Título:
The dynamic action mechanism of small cationic antimicrobial peptides
Autor/es:
J.J LOPEZ CASCALES; ADRIANA D GARRO; R.D.PORASSO; R. D. ENRIZ
Revista:
PHYSICAL CHEMISTRY CHEMICAL PHYSICS
Editorial:
ROYAL SOC CHEMISTRY
Referencias:
Lugar: CAMBRIDGE; Año: 2014 vol. 16 p. 21694 - 21705
ISSN:
1463-9076
Resumen:
Antimicrobial peptides form part of the immune system as protection against the action of external
pathogens. The differences that exist between mammalian and microbial cell membrane architectures
are key aspects of the ability of these peptides to discriminate between pathogens and host cells. Given
that the pathogen membrane is the non-specific target of these cationic peptides, different molecular
mechanisms have been suggested to describe the rules that permit them to distinguish between
pathogens and mammalian cells. In this context, and setting aside the old fashion idea that cationic
peptides act through one mechanism alone, this work will provide insight into the molecular action
mechanism of small antimicrobial peptides, based on molecular dynamics simulations of phospholipid
bilayers that mimic different cell membrane architectures. After measuring different properties of these
lipid bilayers, in the absence and presence of peptides, a four-step action mechanism was suggested on
the basis of the formation of phospholipid rafts induced by the presence of these cationic peptides.
Thus, this work shows how differences in the bending modulus (kb) of these lipid rafts and differences in
the free energy profiles (DG(z)) associated with the insertion of these peptides into these lipid rafts are
key aspects for explaining the action mechanism of these cationic peptides at the molecular level.