化学
低聚物
化学改性
淀粉样蛋白(真菌学)
肽
蛋白质聚集
共价键
荧光
组合化学
生物物理学
生物化学
生物
有机化学
量子力学
物理
无机化学
作者
Xiaogang Qu,Nan Gao,Zhenqi Liu,Haochen Zhang,Chun Li,Dongqin Yu,Jinsong Ren
标识
DOI:10.1002/anie.202115336
摘要
Post-translational modification (PTM) of protein can significantly change protein conformation and function. Inspired by the natural PTM, we present a new approach to inhibit amyloid aggregation by chemical PTM modification. Polyoxometalates (POMs) were used as examples of inhibitors of β-amyloid peptide (Aβ) aggregation to illustrate the chemical PTM method. After the POMs were modified with thiazolidinethione (TZ), the resulting POMD-TZ acted as a chemical PTM agent and could covalently modify Aβ site-selectively at Lys16. Multiple biophysical techniques and biochemical assays have been employed to show the superiority of the chemical PTM method compared to traditional Aβ inhibitors. Since Aβ oligomers are more cytotoxic, we further functionalized POMD-TZ with an Aβ-targeted peptide and a fluorescent probe to obtain an "Aβ oligomer sensitive" probe. The use of PTM agents for the site-directed chemical modification of proteins provides a new way to regulate amyloid aggregation.
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