TITLE:
Spontaneous Unfolding and Refolding of Plantaricin α-Helix in Molecular Dynamics Simulation
AUTHORS:
Shaomin Yan, Guang Wu
KEYWORDS:
Alpha-Helix, Antimicrobial Peptides, Protein Folding, Plantaricin A
JOURNAL NAME:
Computational Molecular Bioscience,
Vol.9 No.1,
March
28,
2019
ABSTRACT: Antimicrobial peptides are promising therapeutic
agents in view of increasing resistance to conventional antibiotics.
Antimicrobial peptides usually fold in α-helical, β-sheet, and
extended/random-coil structures. The α-helical antimicrobial peptides are often unstructured in aqueous
solution but become structured on bacterial membrane. The α-helical structure allows the partitioning into bacterial membrane.
Therefore it is important to understand the mechanism of unfolding and
refolding of α-helical structure in antimicrobial peptides. It is not very easy to
obverse and study the process of unfolding and refolding of α-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.