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Abstract
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Antimicrobial 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.
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