INVESTIGADORES
GARRO Adriana Deolinda
congresos y reuniones científicas
Título:
Dynamic Action Mechanism of Small Antimicrobial
Autor/es:
ADRIANA GARRO; ANA RODRÍGUEZ; RODOLFO PORASSO; RICARDO ENRIZ; JOSÉ LOPEZ CASCALES
Lugar:
Santiago
Reunión:
Congreso; 10th Congress of the World Association of Theoretical and Computational Chemists WATOC; 2014
Resumen:
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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 is a key aspect
in the ability of these peptides to discriminate between pathogen and
host cells. The differences that exist between mammalian and
microbial cell membrane
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
pathogen 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 constants (kb)
of these lipid rafts and differences in the free energy profiles
(G(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 a molecular level.