Can antimicrobial peptides scavenge around a cell in less than a second?
Can antimicrobial peptides scavenge around a cell in less than a second?
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DOI：
10.1016/j.bbamem.2009.08.018
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发表时间：
2010-02-01
影响因子：
3.4
通讯作者：
Cotten, Myriam
中科院分区：
文献类型：
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作者：
Chekmenev, Eduard Y.;Vollmar, Breanna S.;Cotten, Myriam
抗菌肽作为一种具有多种宿主防御功能的多肽，由于其在制药和食品生产中的潜在应用而受到越来越多的关注。虽然它们的作用机制有很多争论，但已经先进的模型共享需要肽动力学的肽-脂质相互作用模式。在这些模型中提出的高度协同和特异性的事件发生之前，肽必须经历一个重要的过程，即沿着膜表面迁移，并从它们在膜上的结合位点递送到功能性能的实际位点。这种现象，这有助于显着的抗菌功能，是知之甚少，主要是由于缺乏实验和计算工具需要评估it.here，我们使用N-15固态核磁共振获得分子水平的数据上的运动的piscidin的两亲性螺旋的磷脂双分子层的表面。这里提出的研究可能有助于更好地理解导致抗菌反应发生的事件的速度。具体而言，从细胞过程的动力学的角度来看，我们讨论的可能性，鱼杀菌素，也许许多其他两亲性抗菌肽的膜表面上的活性可能代表一类快速清除剂，而不是静态的多肽连接到水-脂质界面。(c)2009 Elsevier B. V.保留所有权利。
Antimicrobial peptides, which play multiple host-defense roles, have garnered increased experimental focus because of their potential applications in the pharmaceutical and food production industries. While their mechanisms of action are richly debated, models that have been advanced share modes of peptide-lipid interactions that require peptide dynamics. Before the highly cooperative and specific events suggested in these models take place, peptides must undergo an important process of migration along the membrane surface and delivery from their site of binding on the membrane to the actual site of functional performance. This phenomenon, which contributes significantly to antimicrobial function, is poorly understood, largely due to a lack of experimental and computational tools needed to assess it. Here, we use N-15 solid-state nuclear magnetic resonance to obtain molecular level data on the motions of piscidin's amphipathic helices on the surface of phospholipid bilayers. The studies presented here may help contribute to a better understanding of the speed at which the events that lead to antimicrobial response take place. Specifically, from the perspective of the kinetics of cellular processes, we discuss the possibility that piscidins and perhaps many other amphipathic antimicrobial peptides active on the membrane surface may represent a class of fast scavengers rather than static polypeptides attached to the water-lipid interface. (c) 2009 Elsevier B.V. All rights reserved.