Department of Chemistry, Fordham University, 441 East Fordham Road, Bronx, NY 10458, USA.
J Pept Sci. 2011 Jan;17(1):14-23. doi: 10.1002/psc.1284. Epub 2010 Sep 2.
In this work we have probed the interactions of the amyloid Aβ(1-42) peptide with self-assembled nanospheres. The nanospheres were formed by self-assembly of a newly developed bolaamphiphile bis(N-alpha-amido-methionine)-1,8 octane dicarboxylate under aqueous conditions. It was found that the interactions of the Aβ(1-42) peptide with the nanospheres were concentration as well as pH dependent and the peptide largely adopts a random coil structure upon interacting with the nanospheres. Further, upon incorporation with the nanospheres, we observed a relative diminution in the aggregation of Aβ(1-42) at low concentrations of Aβ(1-42). The interactions between the nanospheres and the Aβ(1-42) peptide were investigated by atomic force microscopy, transmission electron microscopy, circular dichroism, FTIR and fluorescence spectroscopy, and the degree of fibrillation in the presence and absence of nanospheres was monitored by the Thioflavine T assay. We believe that the outcome from this work will help further elucidate the binding properties of Aβ peptide as well as designing nanostructures as templates for further investigating the nucleation and fibrillation process of Aβ-like peptides.
在这项工作中，我们研究了淀粉样蛋白 Aβ(1-42)肽与自组装纳米球的相互作用。纳米球是由新开发的双(N-酰胺基甲硫氨酸)-1,8-辛二羧酸酯 bolaamphiphile 在水相条件下自组装形成的。结果发现，Aβ(1-42)肽与纳米球的相互作用既依赖于浓度又依赖于 pH 值，并且当肽与纳米球相互作用时，它主要采用无规卷曲结构。此外，我们观察到，在 Aβ(1-42)的低浓度下，与纳米球结合后，Aβ(1-42)的聚集相对减少。通过原子力显微镜、透射电子显微镜、圆二色性、FTIR 和荧光光谱研究了纳米球与 Aβ(1-42)肽之间的相互作用，并通过 Thioflavine T 测定监测了有无纳米球存在时的纤维形成程度。我们相信，这项工作的结果将有助于进一步阐明 Aβ 肽的结合特性，并设计纳米结构作为进一步研究 Aβ 样肽成核和纤维形成过程的模板。
