Antimicrobial peptides are promising therapeutic
agents in view of increasing resistance to conventional antibiotics.
Antimicrobial peptides usually fold inα-helical, β-sheet, and
extended/random-coil structures. Theα-helical antimicrobial peptides are often unstructured in aqueous
solution but become structured on bacterial membrane. Theα-helical structure allows the partitioning into bacterial membrane.
Therefore it is important to understand the mechanism of unfolding and
refolding ofα-helical structure in antimicrobial peptides. It is not very easy to
obverse and study the process of unfolding and refolding ofα-helical antimicrobial peptides because of their rapidity. Therefore,
molecular simulation provides a way to observe and explain this phenomenon.
Plantaricin A is a 26 amino-acid antimicrobial pheromone peptide and can
spontaneously unfold and refold under physiological condition. This study
demonstrated the unfolding and refolding of plantaricin A by means of molecular
simulation, and its mechanism was discussed with its implication to the
Levinthal paradox.
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