Influence of antimicrobial peptides on the formation of nonlamellar lipid mesophases
Influence of antimicrobial peptides on the formation of nonlamellar lipid mesophases
复制标题
DOI：
10.1016/j.bbamem.2008.05.014
复制
发表时间：
2008-10-01
影响因子：
3.4
通讯作者：
Pabst, Georg
中科院分区：
文献类型：
--
作者：
Hickel, Andrea;Danner-Pongratz, Sabine;Pabst, Georg
采用差示扫描量热法和小角X射线衍射法研究了蜂毒肽（Melittin，Mel）、保护素-1（Protegrin-1，PG-1）、肽基甘氨酰亮氨酸羧酰胺（Pegtidyl-glycylleucine-carboxyamide，PGLa）和短杆菌肽S（Gramicidin S，GS）-4种不同二级和三级结构的抗菌肽对棕榈酰油酰磷脂酰乙醇胺（POPE）片层-非片层转变的影响。研究的肽没有导致纯POPE在高温下观察到的倒置六方相的形成。相反，立方相或层状相被稳定到不同程度。GS是最有效的诱导立方相，而梅尔完全稳定的层状相。在PG-1和PGLa存在下，POPE的行为介于GS和Mel之间。除了已知的膜弹性的作用，我们提出了两种机制，这导致稳定的层状相：静电排斥和脂质/肽孔的形成。这两种机制都阻止了形成作为立方相前体的倒置六方相或融合孔所需的跨膜接触。(c)2008 Elsevier B. V.保留所有权利。
We have studied the influence of four antimicrobial peptides of different secondary and ternary structure melittin (Mel), protegrin-1 (PG-1), peptidyl-glycylleucine-carboxyamide (PGLa), and gramicidin S (GS) - on the lamellar-to-nonlamellar transition of palmitoyloleoyl phosphatidylethanolamine (POPE) applying differential scanning calorimetry and small-angle X-ray diffraction. None of the peptides studied led to the formation of an inverted hexagonal phase observed for pure POPE at high temperatures. Instead either cubic or lamellar phases were stabilized to different degrees. GS was most effective in inducing a cubic phase, whereas Mel fully stabilized the lamellar phase. The behavior of POPE in the presence of PG-1 and PGLa was intermediate to GS and Mel. In addition to the known role of membrane elasticity we propose two mechanisms, which cause stabilization of the lamellar phase: electrostatic repulsion and lipid/peptide pore formation. Both mechanisms prevent transmembrane contact required to form either an inverted hexagonal phase or fusion pores, as precursors of the cubic phase. (c) 2008 Elsevier B.V. All rights reserved.