Sánchez Rosa, Martínez Javier, Montoya Laura, Castellanos Milagros, Gasset Maria
Institute of Physical Chemistry "Rocasolano", Spanish National Research Council (CSIC), Madrid, Spain.
Faculdade de Ciências, Departamento de Química e Bioquímica, Biosystems and Integrative Sciences Institute, Universidade de Lisboa, Lisbon, Portugal.
Methods Mol Biol. 2018;1779:197-207. doi: 10.1007/978-1-4939-7816-8_13.
Amyloid formation is basically featured by a protein-protein interaction in which the reacting regions are the segments assembling into cross β-sheets. To identify these segments both theoretical and experimental tools have been developed. Here, we focus on the use of peptide arrays to probe the binding of several amyloid-specific probes such as the OC and A11 anti-amyloid conformation-selective antibodies and of monomers and preformed fibrils. These arrays use libraries containing partly overlapping peptides derived from the sequence of Gad m 1, the major allergen from Atlantic cod, which forms amyloids under gastrointestinal relevant conditions.
淀粉样蛋白形成的基本特征是蛋白质-蛋白质相互作用，其中反应区域是组装成交叉β-折叠的片段。为了识别这些片段，已经开发了理论和实验工具。在这里，我们重点关注使用肽阵列来探测几种淀粉样蛋白特异性探针的结合，如OC和A11抗淀粉样蛋白构象选择性抗体以及单体和预形成的纤维。这些阵列使用包含部分重叠肽的文库，这些肽来自大西洋鳕鱼的主要过敏原Gad m 1的序列，该过敏原在胃肠道相关条件下形成淀粉样蛋白。
