Laboratory for Cellulose and Wood Materials, Empa, Überlandstrasse 129, 8600 Dübendorf, Switzerland.
Institute of Food Nutrition and Health, ETH Zürich, Schmelzbergstrasse 7, 8092 Zürich, Switzerland.
Nanoscale. 2023 Nov 16;15(44):17785-17792. doi: 10.1039/d3nr02109b.
Proteins in solution tend to coat solid surfaces upon exposure. Depending on the nature of the surface, the environmental conditions, and the nature of the protein these adsorbed proteins may self-assemble into ordered, fibre-like structures called amyloids. Nanoparticulate surfaces, with their high surface to volume ratio, are particularly favourable to amyloid formation. Most prior research has focussed on either inorganic or organic nanoparticles in solution. In this research, we instead focus on aerogels created from TEMPO-oxidized cellulose nanofibers (TO-CNF) to serve as bio-based, three-dimensional amyloid templates with a tuneable surface chemistry. Previous research on the use of cellulose as a protein adsorption template has shown no evidence of a change in the secondary protein structure. Herein, however, with the aid of the reducing agent TCEP, we were able to induce the formation of amyloid-like 'worms' on the surface of TO-CNF aerogels. Furthermore, we demonstrate that the addition of the TO-CNF aerogel can also induce bulk aggregation under conditions where it previously did not exist. Finally, we show that the addition of the aerogel increases the rate of 'worm' formation in conditions where previous research has found a long lag-phase. Therefore, TO-CNF aerogels are shown to be excellent templates for inducing ordered protein aggregation.
溶液中的蛋白质在暴露于固体表面时往往会附着在表面上。根据表面的性质、环境条件和蛋白质的性质,这些吸附的蛋白质可能会自组装成有序的、纤维状结构,称为淀粉样蛋白。具有高表面积与体积比的纳米颗粒表面特别有利于淀粉样蛋白的形成。大多数先前的研究都集中在溶液中的无机或有机纳米颗粒上。在这项研究中,我们转而关注由 TEMPO 氧化的纤维素纳米纤维(TO-CNF)制成的气凝胶,将其作为具有可调表面化学性质的基于生物的三维淀粉样蛋白模板。先前关于纤维素作为蛋白质吸附模板的研究表明,蛋白质的二级结构没有变化。然而,在此,在还原剂 TCEP 的帮助下,我们能够在 TO-CNF 气凝胶表面诱导形成类似淀粉样的“蠕虫”。此外,我们证明,在以前不存在的条件下,添加 TO-CNF 气凝胶也可以诱导体相聚集。最后,我们表明,在先前的研究发现长滞后期的条件下,添加气凝胶会增加“蠕虫”形成的速度。因此,TO-CNF 气凝胶被证明是诱导有序蛋白质聚集的极好模板。