%0 Journal Article
%T Spontaneous Unfolding and Refolding of Plantaricin ¦Á-Helix in Molecular Dynamics Simulation
%A Shaomin Yan
%A Guang Wu
%J Computational Molecular Bioscience
%P 27-39
%@ 2165-3453
%D 2019
%I Scientific Research Publishing
%R 10.4236/cmb.2019.91003
%X Antimicrobial peptides are promising therapeutic
agents in view of increasing resistance to conventional antibiotics.
Antimicrobial peptides usually fold in ¦Á-helical, ¦Â-sheet, and
extended/random-coil structures. The ¦Á-helical antimicrobial peptides are often unstructured in aqueous
solution but become structured on bacterial membrane. The ¦Á-helical structure allows the partitioning into bacterial membrane.
Therefore it is important to understand the mechanism of unfolding and
refolding of ¦Á-helical structure in antimicrobial peptides. It is not very easy to
obverse and study the process of unfolding and refolding of ¦Á-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.
%K Alpha-Helix
%K Antimicrobial Peptides
%K Protein Folding
%K Plantaricin A
%U http://www.scirp.org/journal/PaperInformation.aspx?PaperID=91482