%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