Peptide Nanospheres Self-Assembled from a Modified β-Annulus Peptide of Sesbania Mosaic Virus
Peptide Nanospheres Self-Assembled from a Modified β-Annulus Peptide of Sesbania Mosaic Virus
复制标题
由田菁花叶病毒修饰的β-环肽自组装的肽纳米球
DOI：
10.1002/bip.22774
复制
发表时间：
2016
期刊：
影响因子：
--
通讯作者：
N. Kimizuka
中科院分区：
文献类型：
--
作者：
K. Matsuura;Y. Mizuguchi;N. Kimizuka
合成了一种新的田菁花叶病毒β-环肽，其C末端带有FKFE序列，并研究了其在水中的自组装行为。动态光散射和透射电子显微镜表明，带有FKFE序列的β-环肽在pH 3.8的水中自组装成约30 nm的纳米球，而没有FKFE序列的β-环肽仅提供不规则的聚集体。肽纳米球具有一定的临界聚集浓度（CAC = 26 μM），在该浓度以上，纳米球的尺寸几乎不受肽浓度的影响。肽纳米球的形成受pH值影响显着；该肽在 pH 2.2 时不形成任何组装体，而在 pH 6.4-11.6 时形成较大的聚集体。 © 2015 Wiley periodicals, Inc. 生物聚合物（Pept Sci）106：470–475，2016。
A novel β‐annulus peptide of Sesbania mosaic virus bearing an FKFE sequence at the C terminus was synthesized, and its self‐assembling behavior in water was investigated. Dynamic light scattering and transmission electron microscopy showed that the β‐annulus peptide bearing an FKFE sequence self‐assembled into approximately 30 nm nanospheres in water at pH 3.8, whereas the β‐annulus peptide without the FKFE sequence afforded only irregular aggregates. The peptide nanospheres possessed a definite critical aggregation concentration (CAC = 26 μM), above which the size of nanospheres were nearly unaffected by the peptide concentration. The formation of peptide nanospheres was significantly affected by pH; the peptide did not form any assemblies at pH 2.2, whereas larger aggregates were formed at pH 6.4–11.6. © 2015 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 106: 470–475, 2016.