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.
Highlights
Antimicrobial peptides are promising therapeutic agents, because they can act on Gram-positive/negative bacteria, protozoa, yeast, fungi, viruses, etc., and because they come from almost all organisms [1] [2]
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
The unfolding and refolding of plantaricin A were conducted in molecular dynamics simulation, because of its ready switch between folded and unfolded α-helical structures
Summary
Antimicrobial peptides are promising therapeutic agents, because they can act on Gram-positive/negative bacteria, protozoa, yeast, fungi, viruses, etc., and because they come from almost all organisms [1] [2]. Besides having a great diversity in their function, antimicrobial peptides have a great diversi-. Of three thousands of antimicrobial peptides [6], α-helical structure accounts 14.88%, β-sheet structure accounts 2.69%, whereas the majority (58.85%) are unknown structures and the rest are mixed structures. Α-helix is the most important structure in antimicrobial peptides. Amphipathicity and hydrophobicity, is the most important factor in antimicrobial peptides for their activity [3], the α-helical structure produces distinct membrane-bound amphipathic conformation [7] and allows its partitioning into bacterial membrane
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