Electrostatically tuned rate of peptide self-assembly resolved by multiple particle tracking.
Electrostatically tuned rate of peptide self-assembly resolved by multiple particle tracking.
复制标题
DOI：
10.1039/b700434f
复制
发表时间：
2007-08
期刊：
影响因子：
3.4
通讯作者：
T. Savin;P. Doyle
中科院分区：
文献类型：
--
作者：
T. Savin;P. Doyle
由寡肽自组装形成的水凝胶被广泛研究用于生物医学应用。它们凝胶化的动力学，以及控制组装速率的力的定量描述尚未得到解决。我们在这里报告了使用多粒子跟踪来测量模型肽FKFEFKFE （KFE8）的自组装动力学。KFE8形成明确的β-薄片中间体，经常被用作在水溶液中形成纤维网络的模型肽系统。我们发现，将该体系的pH从3.5增加到4.0，KFE8凝胶化的时间几乎减少了100倍，从小时到分钟。在不同pH值下进行的测量之间具有显著的自相似性，这表明，尽管pH值的增加加速了凝胶化，但凝胶化遵循不变的机制。我们根据Derjaguin-Landau-Verwey-Overbeek （DLVO）理论，利用驱动自组装的相互作用的简单模型，提出了胶凝时间数量级的半定量解释。这种理解对于当前和未来的治疗应用（药物传递）的发展是重要的。
Hydrogels formed from the self-assembly of oligopeptides are being extensively studied for biomedical applications. The kinetics of their gelation, as well as a quantitative description of the forces controlling the rate of assembly has not yet been addressed. We report here the use of multiple particle tracking to measure the self-assembly kinetics of the model peptide FKFEFKFE (KFE8). KFE8 forms well-defined β-sheet intermediates and is often used as a model peptide system that forms a fibrous network in aqueous solvent. We find that increasing the pH of this system from 3.5 to 4.0 decreases the time of KFE8 gelation by almost hundredfold, from hours to minutes. A remarkable self-similarity between measurements performed at different pH suggests that, although accelerated by the pH increase, gelation follows an invariable mechanism. We propose a semi-quantitative interpretation for the order of magnitudes of gelation time using a simple model for the interaction driving the self-assembly in terms of the Derjaguin-Landau-Verwey-Overbeek (DLVO) theory. Such understanding is important for the development of current and future therapeutic applications ( drug delivery).