Molecular dynamics studies of transportan 10 (tp10) interacting with a POPC lipid bilayer.
Molecular dynamics studies of transportan 10 (tp10) interacting with a POPC lipid bilayer.
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DOI：
10.1021/jp107763b
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发表时间：
2011-02-10
影响因子：
3.3
通讯作者：
Lee, Hee-Seung
中科院分区：
文献类型：
--
作者：
Dunkin, Christina M.;Pokorny, Antje;Almeida, Paulo F.;Lee, Hee-Seung
我们进行了一系列分子动力学模拟来研究转运蛋白10(Tp10)与两性离子POPC双层之间相互作用的性质。Tp10是一种两亲性细胞穿透性多肽，其净正电荷为+5，膜表面具有α-螺旋二级结构。研究表明，tp10优先结合在膜表面，其疏水侧面向疏水脂核。这种取向允许带有正电荷的长侧链的Lys残基在插入过程中停留在极性环境中。模拟表明，Lys-磷酸盐桥是决定多肽在界面区域的取向以及稳定多肽-膜相互作用的关键因素。赖氨酸和磷酸基团之间的静电吸引也被认为是tp10跨膜转运的主要瓶颈。
We performed a series of molecular dynamics simulations to study the nature of interactions between transportan 10 (tp10) and a zwitterionic POPC bilayer. Tp10 is an amphipathic cell-penetrating peptide with a net positive charge of +5 and is known to adopt an α-helical secondary structure on the surface of POPC membranes. The study showed that tp10 preferentially binds to the membrane surface with its hydrophobic side facing the hydrophobic lipid core. Such orientation allows Lys residues, with positively charged long side chains, to stay in the polar environment during the insertion process. The simulations revealed that the Lys–phosphate salt bridge is a key factor in determining the orientation of the peptide in the interfacial region as well as in stabilizing the peptide-membrane interaction. The electrostatic attraction between Lys and phosphate groups is also believed to be the main bottleneck for the translocation of tp10 across the membrane.
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