期刊
BIOPHYSICAL JOURNAL
卷 101, 期 5, 页码 1238-1247出版社
CELL PRESS
DOI: 10.1016/j.bpj.2011.07.023
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资金
- Biotechnology and Biological Sciences Research Council [BB/D010284/1, BB/526502/1]
- Biotechnology and Biological Sciences Research Council Research Equipment Initiative [BB/E012558/1]
- Micromass UK Ltd.
- University of Leeds
- BBSRC [BB/D010284/1, BB/E012558/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/D010284/1, BB/E012558/1] Funding Source: researchfish
beta(2)-Microglobulin is a 99-residue protein with a propensity to form amyloid-like fibrils in vitro which exhibit distinct morphologies dependent on the solution conditions employed. Here we have used ion mobility spectrometry-mass spectrometry to characterize the oligomeric species detected during the formation of worm-like fibrils of beta(2)-microglobulin at pH 3.6. Immediately upon sample dissolution, beta(2)-microglobulin monomer and oligomers-the latter ranging in size from dimer to hexamer are present as a pool of rapidly interconverting species. Increasing the ionic strength of the solution initiates fibril formation without a lag-phase whereupon these oligomers become more stable and higher-order species (7-mer to >14-mer) are observed. The oligomers detected have collision cross-sectional areas consistent with a linearly stacked assembly comprising subunits of native-like volume. The results provide insights into the identity and properties of the transient, oligonneric intermediates formed during assembly of worm-like fibrils and identify species that differ significantly from the oligomers previously characterized during the nucleated assembly of long, straight fibrils. The data presented demonstrate the interrelationship between different fibril-forming pathways and identify their points of divergence.
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