ci6b00693_si_001.pdf (1.09 MB)
Identification of the Crucial Residues in the Early Insertion of Pardaxin into Different Phospholipid Bilayers
journal contribution
posted on 2017-03-16, 00:00 authored by Majid Jafari, Faramarz Mehrnejad, Raheleh Aghdami, Nader Chaparzadeh, Zahra Razaghi Moghadam Kashani, Farahnoosh DoustdarAntimicrobial
peptides (AMPs) are part of the innate host defense system, and they
are produced by living organisms to defend themselves against infections.
Pardaxin is a cationic AMP with antimicrobial and antitumor activities
that has potential to be used as a novel antibiotic or for drug delivery
in cancer therapy. This peptide acts on the membrane of target cells
and can lead to lysis using different mechanisms of action. Here,
we conducted 4.5 μs all-atom molecular dynamics
(MD) simulations to determine the critical fragments and residues
of Pardaxin for early insertion into different lipid bilayers. Our
results revealed that the N-terminal domain of the peptide, particularly
the Phe 2 and (/or) Phe 3 residues, has a crucial role in early insertion,
independent of the type of lipid bilayers.