Institute of Materials Research and Engineering, A*Star, 2 Fusionopolis Way, Innovis, Singapore 138634, Singapore.
CSL Biotherapies, 189-209 Camp Road, Broadmeadows, Victoria 3047, Australia.
Int J Biol Macromol. 2018 Jan;106:30-38. doi: 10.1016/j.ijbiomac.2017.07.171. Epub 2017 Aug 1.
Amyloid fibrils are associated with the pathogenesis of protein misfolding diseases such as Alzheimer's disease. These fibrils typically exhibit different morphologies when grown in vitro, and this has been known to affect their biological properties and cytotoxicity. The formation kinetics and resultant morphology of fibrils formed from the model proteins Bovine Insulin and Hen Egg White Lysozyme have been measured. We show that the presence of gum arabic and pectin during fibril formation cause the amyloid fibrils formed to associate into higher order fibrillar aggregates. It is postulated that the carbohydrates act as a template to promote inter-fibril association, resulting in larger, thicker fibrils. This observation provides some insight into the differences in growing amyloid fibrils in vitro in the absence or presence of other high molecular weight compounds. Furthermore, these findings suggest a method of tailoring fibril structure for applications in nanotechnology and bio-template applications.
淀粉样纤维与蛋白质错误折叠疾病（如阿尔茨海默病）的发病机制有关。这些纤维在体外生长时通常表现出不同的形态，这已被证明会影响它们的生物学特性和细胞毒性。已经测量了从模型蛋白牛胰岛素和鸡卵清溶菌酶形成的纤维的形成动力学和所得形态。我们表明，在纤维形成过程中存在阿拉伯树胶和果胶会导致形成的淀粉样纤维缔合成更高阶的纤维状聚集体。据推测，碳水化合物作为模板促进纤维间的缔合，从而形成更大、更厚的纤维。这一观察结果为研究在不存在或存在其他高分子量化合物的情况下体外生长淀粉样纤维的差异提供了一些线索。此外，这些发现为在纳米技术和生物模板应用中定制纤维结构提供了一种方法。
