Spontaneous Unfolding and Refolding of Plantaricin α-Helix in Molecular Dynamics Simulation

• 作者: Guang Wu Shaomin Yan
• 来源期刊: 计算分子生物学(英文)
• 学科: 医学
• 关键词: ALPHA-HELIX Antimicrobial Peptides Protein FOLDING Plantaricin A
• 年，卷（期）: 2019,（1）
• 页码范围: 27-39
• 页数: 13页
• 分类号: R73

摘要

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.