ArticleRapid communications in mass spectrometry : RCM2006
Investigating the structural properties of amyloid-like fibrils formed in vitro from beta2-microglobulin using limited proteolysis and electrospray ionisation mass spectrometry.
Article in Rapid communications in mass spectrometry : RCM, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 61 citations in OpenAlex.
- Amyloid fibrils degradation: the pathway to recovery or aggravation of the disease?Frontiers in molecular biosciences · 2023Article
- Review
- Trypsin Induced Degradation of Amyloid Fibrils.International journal of molecular sciences · 2021Article
- Looking Beyond the Core: The Role of Flanking Regions in the Aggregation of Amyloidogenic Peptides and Proteins.Frontiers in neuroscience · 2020Review
- The structure of a βNature communications · 2018Article
- Secondary structure in the core of amyloid fibrils formed from human β₂m and its truncated variant ΔN6.Journal of the American Chemical Society · 2014Article
- Expanding the repertoire of amyloid polymorphs by co-polymerization of related protein precursors.The Journal of biological chemistry · 2013Article
- Structure and dynamics of oligomeric intermediates in β2-microglobulin self-assembly.Biophysical journal · 2011Article
- Intermolecular alignment in β2-microglobulin amyloid fibrils.Journal of the American Chemical Society · 2010Article
- Magic angle spinning NMR analysis of beta2-microglobulin amyloid fibrils in two distinct morphologies.Journal of the American Chemical Society · 2010Article
- Mass spectrometry and the amyloid problem--how far can we go in the gas phase?Journal of the American Society for Mass Spectrometry · 2010Article
- Stacked sets of parallel, in-register beta-strands of beta2-microglobulin in amyloid fibrils revealed by site-directed spin labeling and chemical labeling.The Journal of biological chemistry · 2010Article
- The 8 and 5 kDa fragments of plasma gelsolin form amyloid fibrils by a nucleated polymerization mechanism, while the 68 kDa fragment is not amyloidogenic.Biochemistry · 2009Article
- Globular tetramers of beta(2)-microglobulin assemble into elaborate amyloid fibrils.Journal of molecular biology · 2009Article
- Probing dynamics within amyloid fibrils using a novel capping method.Angewandte Chemie (International ed. in English) · 2009Article
- A common beta-sheet architecture underlies in vitro and in vivo beta2-microglobulin amyloid fibrils.The Journal of biological chemistry · 2008Article
- Time-resolved limited proteolysis of mitogen-activated protein kinase-activated protein kinase-2 determined by LC/MS only.Journal of the American Society for Mass Spectrometry · 2008Article
- Fibril growth kinetics reveal a region of beta2-microglobulin important for nucleation and elongation of aggregation.Journal of molecular biology · 2008Article
- Dissociation from the oligomeric state is the rate-limiting step in fibril formation by kappa-casein.The Journal of biological chemistry · 2008Article
- Folding versus aggregation: polypeptide conformations on competing pathways.Archives of biochemistry and biophysics · 2008Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The protein beta(2)-microglobulin (beta(2)m) aggregates to form classical amyloid fibrils in patients undergoing long-term haemodialysis. Amyloid-like fibrils with a cross-beta fold can also be formed from wild-type beta(2)m under acidic conditions in vitro. The morphology of such fibrils depends critically on the conditions used: incubation of beta(2)m in low ionic strength buffers at pH 2.5 results in the formation of long (microm), straight fibrils while, at pH 3.6, short (<500 nm) fibrils form. At higher ionic strengths (0.2-0.4 M) at pH 1.5-3.6, the fibrils have a distinct curved and nodular morphology. To determine the conformational properties of beta(2)m within in vitro fibrils of different morphologies, limited proteolysis of each fibril type using pepsin was performed and the resulting peptide fragments identified by tandem mass spectrometry. For comparison, the proteolytic degradation patterns of monomeric beta(2)m and seven synthetic peptides spanning the entire sequence of the intact protein were similarly analysed. The results show that fibrils with different morphologies result in distinct digestion patterns. While the curved, worm-like fibrils are relatively weakly protected from proteolysis, the long, straight fibrils formed at pH 2.5 at low ionic strength show only a single cut-site at Val9, demonstrating that substantial refolding of the initially acid-denatured and unprotected state of beta(2)m occurs during assembly. The data demonstrate that the organisation of the polypeptide chain in fibrils with different morphological features differs considerably, despite the fact that the fibrils possess a common cross-beta architecture.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.