Raussens Vincent, Waeytens Jehan
Structure et Fonction des Membranes Biologiques, Université libre de Bruxelles, Bruxelles, Belgium.
Institut de Chimie Physique, CNRS UMR8000, Université Paris-Sud, Université Paris-Saclay, Orsay, France.
Methods Mol Biol. 2022;2538:117-129. doi: 10.1007/978-1-0716-2529-3_9.
Atomic force microscopy has been used for decades to study the topography of proteins during aggregation but with a lack of information on the secondary structure. On the contrary, infrared spectroscopy was able to study structural changes during the aggregation, but this analysis is complicated due to the presence of different species in mixtures and the poor spatial (~μm) resolution of the FTIR microscopy. Recently, Professor Alexandre Dazzi combined those techniques in the so-called AFM-IR. This method allows acquiring IR spectra at the nanometric scale and becomes a new standard method for the characterization of amyloid fibrils and, more generally, for the aggregation of proteins.
几十年来，原子力显微镜一直被用于研究蛋白质聚集过程中的形貌，但缺乏关于二级结构的信息。相反，红外光谱能够研究聚集过程中的结构变化，但由于混合物中存在不同的物种以及傅里叶变换红外显微镜的空间分辨率较差（约为微米级），这种分析变得复杂。最近，亚历山大·达齐教授将这些技术结合在所谓的原子力显微镜 - 红外光谱联用技术（AFM - IR）中。这种方法能够在纳米尺度获取红外光谱，并成为表征淀粉样纤维以及更普遍地用于蛋白质聚集研究的一种新的标准方法。
