Data set for the Commun. Chem. article by Paul et al. with the title "13C- and 15N-labeling of amyloid-β and inhibitory polypeptides to study their interaction via nanoscale infrared spectroscopy"

The data published here are the basis for the article by Paul et al. in Commun. Chem. with the title <em>13C- and 15N-labeling of amyloid-β and inhibitory polypeptides to study their interaction via nanoscale infrared spectroscopy</em> and for the Research Square preprint by Paul et al. with DOI: 10.21203/rs.3.rs-2141341/v1 and title <em>13C-isotope-editing of nanoscale infrared images reveals the action of an inhibi­tory peptide against amyloid-β aggregation</em>. <br> These publications show that 13C, 15N-labeling can be used to discriminate between two peptides in nanoscale images of their infrared absorption, even when they have similar secondary structure. We studied different aggregation states of the amyloid-β peptide (Aβ) and its interaction with an inhibitory cell-penetrating peptide (NCAM1-PrP) using scattering-type scanning near-field optical microscopy (s-SNOM). Labeled and unlabeled peptides could be distinguished by comparing images of the optical phase taken at wavenumbers characteristic for either the labeled or the unlabeled peptide. <br> Some of the provided files require particular software to view them: Gwyddion (http://gwyddion.net/) is needed for image files, neaPLOT (attocube) for nano-FTIR spectra, and OPUS (Bruker) for FTIR spectra. Processed neaPLOT files were stored as csv files. OPUS files were converted to txt files but can also be read by Spectragryph (https://www.effemm2.de/spectragryph/about.html), which is free for private and academic use.

此处发布的数据，是Paul等人发表于《Commun. Chem.》、题为《通过纳米尺度红外光谱研究淀粉样蛋白-β与抑制性多肽的13C及15N标记及其相互作用》的论文，以及Paul等人发布于Research Square、DOI为10.21203/rs.3.rs-2141341/v1、题为《纳米尺度红外成像的13C同位素编辑技术揭示抑制肽对抗淀粉样蛋白-β聚集的作用》的预印本的核心研究支撑素材。
上述研究成果证实，即便两种多肽拥有相似的二级结构，借助13C、15N标记技术，仍可在其红外吸收的纳米尺度成像中实现有效区分。本研究采用散射型扫描近场光学显微镜（scattering-type scanning near-field optical microscopy, s-SNOM），探究了淀粉样蛋白-β（amyloid-β, Aβ）的不同聚集状态，以及其与抑制性穿膜肽（cell-penetrating peptide, NCAM1-PrP）的相互作用。通过对比在标记多肽与未标记多肽特征波数下采集的光学相位成像结果，可实现标记与未标记多肽样本的区分。
部分提供的文件需使用特定软件方可查看：图像文件需使用Gwyddion（http://gwyddion.net/），纳米傅里叶变换红外（nano-FTIR）光谱需使用neaPLOT（attocube公司产品），傅里叶变换红外（FTIR）光谱需使用OPUS（Bruker公司产品）。经处理的neaPLOT文件以csv格式存储。OPUS格式文件已转换为txt格式，也可通过Spectragryph（https://www.effemm2.de/spectragryph/about.html）读取，该软件面向个人与学术用户免费开放。