溶菌酶
淀粉样蛋白(真菌学)
背景(考古学)
化学
蛋白质折叠
生物物理学
霍夫迈斯特系列
蛋白质聚集
折叠(DSP实现)
微尺度化学
盐(化学)
纳米技术
生物化学
材料科学
生物
有机化学
无机化学
古生物学
数学教育
工程类
电气工程
数学
作者
Hussein Chaaban,Jijo J. Vallooran,Marco van de Weert,Vito Foderà
标识
DOI:10.1021/acs.jpclett.2c00182
摘要
Salt ions are considered among the major determinants ruling protein folding, stability, and self-assembly in the context of amyloid-related diseases, protein drug development, and functional biomaterials. Here, we report that Hofmeister ions not only determine the rate constants of the aggregation reaction for human insulin and hen egg white lysozyme but also control the generation of a plethora of amyloid-like morphologies ranging from the nanoscale to the microscale. We anticipate that the latter is a result of a balance between colloidal and conformational stability combined with an ion-specific effect and highlight the importance of salt ions in controlling the biological functions of protein aggregates.
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