The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Insights into the Mechanism of Aggregation and Fibril Formation from Bovine Serum Albumin
Abstract
We have investigated the fibrillation propensity of different conformational isomers of an archetypal, all α-helical protein, namely, bovine serum albumin (BSA), under different pH conditions and ionic strengths using fluorescence and circular dichroism (CD) spectroscopy. At low pH and higher protein concentration, the partially folded conformers associate to form oligomers that are converted into ordered amyloid-like fibrils when incubated at elevated temperature. We have elucidated the mechanism of fibril formation, especially the early steps, by monitoring the kinetics of structural changes during the aggregation process. Various structural probes in tandem were utilized to decipher the temporal evolution of both conformational and size changes by measuring the time dependence of fluorescence intensity and anisotropy of intrinsic tryptophans and several extrinsic fluorophores during the aggregation. Additionally, CD spectroscopy was utilized to monitor the changes in protein secondary structural content during fibrillation. Our findings suggest that the conformational conversion occurs in the oligomers that serve as precursors to amyloid fibrils and precedes the overall fibrillar growth.
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Cites
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
Bucciantini, M., Giannoni, E., Chiti, F., Baroni, F., Formigli, L., Zurdo, J., Taddei, N., Ramponi, G., Dobson, C. M., & Stefani, M. (2002) · Nature · doi:10.1038/416507a · Cited by 2,434
[18] Quantification of β-sheet amyloid fibril structures with thioflavin T
LeVine, H. (1999) · Methods in Enzymology · doi:10.1016/s0076-6879(99)09020-5 · Cited by 1,365
Rationalization of the effects of mutations on peptide andprotein aggregation rates
Chiti, F., Stefani, M., Taddei, N., Ramponi, G., & Dobson, C. M. (2003) · Nature · doi:10.1038/nature01891 · Cited by 1,072
Cited by
Cao, Y., & Mezzenga, R. (2019) · Advances in Colloid and Interface Science · doi:10.1016/j.cis.2019.05.002 · Cited by 649
Sabaté del Río, J., Henry, O. Y. F., Jolly, P., & Ingber, D. E. (2019) · Nature Nanotechnology · doi:10.1038/s41565-019-0566-z · Cited by 450
Protein aggregation – Mechanisms, detection, and control
Wang, W., & Roberts, C. J. (2018) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2018.08.043 · Cited by 299
Metadata
- Authors
- Bhattacharya, M., Jain, N., & Mukhopadhyay, S.
- Venue
- The Journal of Physical Chemistry B
- Publisher
- American Chemical Society (ACS)
- Published
- 2011-03-21
- Volume
- 115
- Issue
- 14
- Pages
- 4195-4205
- ISSN
- 1520-5207 (ISSN-L)
- 1520-6106
- OpenAlex
- W1992430893
- Cited by
- 207
- References
- 3
- FWCI
- 4.23
- Type
- journal article
- Language
- en
- Open access
- closed
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