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- W2912258021 abstract "Beta2-microglobulin (b2m) is one of the well-known amyloid forming proteins that cause human degenerative diseases. The mechanism of b2m amyloid formation has been extensively studied for more than few decades, however, the detailed oligomer structures and underlying driving force are still unclear and under intense debate. Remarkably, recent experiments suggest that copper ions play a crucial role in promoting b2m oligomers and facilitating aggregation process. Here, we combine ion mobility mass spectrometry (MS) and molecular dynamics (MD) simulation to investigate possible oligomer structures along the assembly pathway. We found that b2m dimers contain coppers, and two intermolecular salt bridges nearby the copper-binding site play a crucial role in stabilizing b2m dimers. Heterogeneous tetramers, which adopt different sizes and copper-binding states, are the key elements for initiating further amyloid formation. Upon losing coppers, one type of tetramers transforms to a pre-polymer state that is assumed to be the building block of b2m polymer. The polymer shows a worm-like structure consisting of native-like monomers, which is consistent with previous NMR and MS studies. In addition, two distinct binding interfaces between native-like monomers play an important role in maintaining both the rigidity and flexibility of the polymer. Based on the structural information of b2m oligomer states that we observed, a copper-induced assembly pathway is then proposed. This suggests that, by designing a proper salt bridge blocker to prevent b2m dimer formation, a promising treatment for b2m related amyloidosis would be established in a near future." @default.
- W2912258021 created "2019-02-21" @default.
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- W2912258021 date "2019-02-01" @default.
- W2912258021 modified "2023-09-30" @default.
- W2912258021 title "Towards Understanding Amyloid Formation Mechanism of Beta2-Microglobulin Induced by Copper Ions" @default.
- W2912258021 doi "https://doi.org/10.1016/j.bpj.2018.11.1073" @default.
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