Spontaneous Unfolding and Refolding of Plantaricin α-Helix in Molecular Dynamics Simulation
Open Access
- 1 January 2019
- journal article
- Published by Scientific Research Publishing, Inc. in Computational Molecular Bioscience
- Vol. 09 (01), 27-39
- https://doi.org/10.4236/cmb.2019.91003
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.Keywords
This publication has 1 reference indexed in Scilit:
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