Journal
BIOPHYSICAL CHEMISTRY
Volume 125, Issue 2-3, Pages 350-359Publisher
ELSEVIER
DOI: 10.1016/j.bpc.2006.09.010
Keywords
protein aggregation; aggregation kinetics; amyloid; fibrils
Funding
- NIGMS NIH HHS [R01 GM070919-01A2, R01 GM070919] Funding Source: Medline
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We have investigated the aggregation of protein L in 25% (vol/vol) TFE and 10 mM HCl. Under both conditions, aggregates adopt a fibrillar structure and bind dyes Congo Red and Thioflavin T consistent with the presence of amyloid fibrils. The kinetics of aggregation in 25% TFE suggest a linear-elongation mechanism with critical nucleus size of either two or three monomers. Aggregation kinetics in 10 mM HCl show a prolonged lag phase prior to a rapid increase in aggregation. The lag phase is time-dependent, but the time dependence can be eliminated by the addition of pre-formed seeds. Disaggregation studies show that for aggregates formed in TFE, aggregate stability is a strong function of aggregate age. For example, after 200 min of aggregation, 40% of the aggregation reaction is irreversible, while after 3 days over 60% is irreversible. When the final concentration of the denaturant, TFE, is reduced from 5% to 0, the amount of reversible aggregation doubles. Disaggregation studies of aggregates formed in TFE and 10 mM HCl reveal a complicated effect of pH on aggregate stability. (c) 2006 Elsevier B.V. All rights reserved.
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