Technical and Macromolecular Chemistry, Paderborn University, Warburger Str. 100, 33098 Paderborn, Germany.
Int J Mol Sci. 2021 May 13;22(10):5142. doi: 10.3390/ijms22105142.
The effects that solid-liquid interfaces exert on the aggregation of proteins and peptides are of high relevance for various fields of basic and applied research, ranging from molecular biology and biomedicine to nanotechnology. While the influence of surface chemistry has received a lot of attention in this context, the role of surface topography has mostly been neglected so far. In this work, therefore, we investigate the aggregation of the type 2 diabetes-associated peptide hormone hIAPP in contact with flat and nanopatterned silicon oxide surfaces. The nanopatterned surfaces are produced by ion beam irradiation, resulting in well-defined anisotropic ripple patterns with heights and periodicities of about 1.5 and 30 nm, respectively. Using time-lapse atomic force microscopy, the morphology of the hIAPP aggregates is characterized quantitatively. Aggregation results in both amorphous aggregates and amyloid fibrils, with the presence of the nanopatterns leading to retarded fibrillization and stronger amorphous aggregation. This is attributed to structural differences in the amorphous aggregates formed at the nanopatterned surface, which result in a lower propensity for nucleating amyloid fibrillization. Our results demonstrate that nanoscale surface topography may modulate peptide and protein aggregation pathways in complex and intricate ways.
固液界面对蛋白质和肽聚集的影响在基础研究和应用研究的各个领域都具有重要意义，从分子生物学和生物医学到纳米技术。虽然表面化学在这方面受到了很多关注，但迄今为止，表面形貌的作用大多被忽视了。在这项工作中，我们研究了与平坦和纳米图案氧化硅表面接触的 2 型糖尿病相关肽激素 hIAPP 的聚集。纳米图案表面是通过离子束辐照产生的，具有约 1.5 和 30nm 的高度和周期性的明确定义的各向异性波纹图案。使用时移原子力显微镜，定量地表征了 hIAPP 聚集体的形态。聚集导致无定形聚集体和淀粉样原纤维的形成，纳米图案的存在导致纤维化延迟和更强的无定形聚集。这归因于在纳米图案表面形成的无定形聚集体中的结构差异，这导致淀粉样原纤维形成的倾向降低。我们的结果表明，纳米级表面形貌可能以复杂而复杂的方式调节肽和蛋白质的聚集途径。
