Cover caption: The aggregation behaviour of peptide fragments of proteins in aqueous solutions with ionic liquids (ILs) could help identify the relationship between IL–protein interactions and structural behaviour of intrinsically disordered proteins in this media. Takekiyo et al. report that the addition of 1‐butyl‐3‐methylimidazolium thiocyanate, but not ethylammonium nitrate, to amyloid β_1–11 peptide (Aβ_1–11) leads to the formation of intermolecular β‐sheet structure (aggregation). Cationic species are associated with the ability to mask the charged residues of β_1–11, whereas anionic species depend on the aggregation selectivity of Aβ_1–11. The results could help develop new antiamyloidogenic agents and alternative solvents for stable protein biomaterials. (doi: 10.1002/pep2.24151)

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封面图片，第112卷，第2期

封面说明：含离子液体（IL）的水溶液中蛋白质的肽片段的聚集行为可能有助于确定IL-蛋白质相互作用与这种介质中固有紊乱蛋白质的结构行为之间的关系。Takekiyo等。报告，加入1-丁基-3-甲基咪唑鎓硫氰酸盐，但不乙基铵硝酸盐，淀粉样蛋白β _1-11肽（A β _1-11）导致分子间的β片层结构（聚集）的形成。阳离子物质与掩盖的电荷的残基的能力相关联的β _1-11，而阴离子物质取决于A的聚合选择性β _1-11。该结果可能有助于开发新的抗淀粉样蛋白生成剂和替代溶剂，用于稳定的蛋白质生物材料。（doi：10.1002 / pep2.24151）