Molecular self-assembly of surfactant-like peptides to form nanotubes and nanovesicles
Molecular self-assembly of surfactant-like peptides to form nanotubes and nanovesicles
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DOI：
10.1073/pnas.072089599
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发表时间：
2002-04-16
影响因子：
11.1
通讯作者：
Zhang, SG
中科院分区：
文献类型：
--
作者：
Vauthey, S;Santoso, S;Zhang, SG
几种表面活性剂样肽经过自组装形成平均直径为30-50纳米的螺旋状纳米管和纳米囊泡。肽单体含有7-8个残基，亲水性头部由天冬氨酸组成，尾部由疏水性氨基酸如丙氨酸、缬氨酸或亮氨酸组成。每个肽的长度约为2 nm，与生物磷脂相似。动态光散射研究显示结构具有非常离散的尺寸。随着时间的推移，分布变得更广，表明一个非常动态的组装和拆卸过程。速冻/深蚀刻样品制备的透射电子显微镜显示出开放式纳米管网络和一些囊泡，后者能够从前者“融合”并“发芽”。结构表现出一定的尾序列偏好。许多可能作为纳米管之间的连接的三向结也被观察到。肽表面活性剂分子的研究对非脂类生物表面活性剂的设计以及对自组装过程的复杂性和动力学的理解具有重要意义。
Several surfactant-like peptides undergo self-assembly to form nanotubes and nanovesicles having an average diameter of 30-50 nm with a helical twist. The peptide monomer contains 7-8 residues and has a hydrophilic head composed of aspartic acid and a tail of hydrophobic amino acids such as alanine, valine, or leucine. The length of each peptide is approximate to2 nm, similar to that of biological phospholipids. Dynamic light-scattering studies showed structures with very discrete sizes. The distribution becomes broader over time, indicating a very dynamic process of assembly and disassembly. Visualization with transmission electron microscopy of quick-freeze/deep-etch sample preparation revealed a network of open-ended nanotubes and some vesicles, with the latter being able to "fuse" and "bud" out of the former. The structures showed some tail sequence preference. Many three-way junctions that may act as links between the nanotubes have been observed also. Studies of peptide surfactant molecules have significant implications in the design of nonlipid biological surfactants and the understanding of the complexity and dynamics of the self-assembly processes.